ID   A0A2V4VIV6_9GAMM        Unreviewed;       545 AA.
AC   A0A2V4VIV6;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   05-DEC-2018, entry version 4.
DE   RecName: Full=Siroheme synthase {ECO:0000256|HAMAP-Rule:MF_01646};
DE   Includes:
DE     RecName: Full=Uroporphyrinogen-III C-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01646};
DE              Short=Urogen III methylase {ECO:0000256|HAMAP-Rule:MF_01646};
DE              EC=2.1.1.107 {ECO:0000256|HAMAP-Rule:MF_01646};
DE     AltName: Full=Uroporphyrinogen III methylase {ECO:0000256|HAMAP-Rule:MF_01646};
DE              Short=UROM {ECO:0000256|HAMAP-Rule:MF_01646};
DE     AltName: Full=SUMT {ECO:0000256|HAMAP-Rule:MF_01646};
DE   Includes:
DE     RecName: Full=Sirohydrochlorin ferrochelatase {ECO:0000256|HAMAP-Rule:MF_01646};
DE              EC=4.99.1.4 {ECO:0000256|HAMAP-Rule:MF_01646};
DE   Includes:
DE     RecName: Full=Precorrin-2 dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01646};
DE              EC=1.3.1.76 {ECO:0000256|HAMAP-Rule:MF_01646};
GN   Name=cysG {ECO:0000256|HAMAP-Rule:MF_01646};
GN   ORFNames=DFP82_106170 {ECO:0000313|EMBL:PYE38765.1};
OS   Psychrobacter fozii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Psychrobacter.
OX   NCBI_TaxID=198480 {ECO:0000313|EMBL:PYE38765.1, ECO:0000313|Proteomes:UP000247746};
RN   [1] {ECO:0000313|EMBL:PYE38765.1, ECO:0000313|Proteomes:UP000247746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5889 {ECO:0000313|EMBL:PYE38765.1,
RC   ECO:0000313|Proteomes:UP000247746};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the
RT   genomes of soil and plant-associated and newly described type
RT   strains.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Multifunctional enzyme that catalyzes the SAM-dependent
CC       methylations of uroporphyrinogen III at position C-2 and C-7 to
CC       form precorrin-2 via precorrin-1. Then it catalyzes the NAD-
CC       dependent ring dehydrogenation of precorrin-2 to yield
CC       sirohydrochlorin. Finally, it catalyzes the ferrochelation of
CC       sirohydrochlorin to yield siroheme. {ECO:0000256|HAMAP-
CC       Rule:MF_01646, ECO:0000256|SAAS:SAAS00971394}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + siroheme = Fe(2+) + sirohydrochlorin;
CC         Xref=Rhea:RHEA:24360, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:58351, ChEBI:CHEBI:60052; EC=4.99.1.4;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01646,
CC         ECO:0000256|SAAS:SAAS01024976};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 S-adenosyl-L-methionine + uroporphyrinogen III = H(+) +
CC         precorrin-2 + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32459,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57308, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:58827, ChEBI:CHEBI:59789; EC=2.1.1.107;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01646,
CC         ECO:0000256|SAAS:SAAS00970331};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin;
CC         Xref=Rhea:RHEA:15613, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58351, ChEBI:CHEBI:58827;
CC         EC=1.3.1.76; Evidence={ECO:0000256|HAMAP-Rule:MF_01646,
CC         ECO:0000256|SAAS:SAAS01024975};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       sirohydrochlorin from precorrin-2: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01646, ECO:0000256|SAAS:SAAS01024981}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC       biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01646, ECO:0000256|SAAS:SAAS00971402}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC       biosynthesis; siroheme from sirohydrochlorin: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01646, ECO:0000256|SAAS:SAAS01024978}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC       biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01646, ECO:0000256|SAAS:SAAS01024982}.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000256|RuleBase:RU003960}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the precorrin
CC       methyltransferase family. {ECO:0000256|HAMAP-Rule:MF_01646,
CC       ECO:0000256|SAAS:SAAS00971398}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the precorrin-2
CC       dehydrogenase / sirohydrochlorin ferrochelatase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01646, ECO:0000256|SAAS:SAAS00971404}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PYE38765.1}.
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DR   EMBL; QJSU01000006; PYE38765.1; -; Genomic_DNA.
DR   UniPathway; UPA00148; UER00222.
DR   UniPathway; UPA00262; UER00211.
DR   Proteomes; UP000247746; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051266; F:sirohydrochlorin ferrochelatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019354; P:siroheme biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd11642; SUMT; 1.
DR   Gene3D; 1.10.8.210; -; 1.
DR   Gene3D; 3.30.950.10; -; 1.
DR   Gene3D; 3.40.1010.10; -; 1.
DR   HAMAP; MF_01646; Siroheme_synth; 1.
DR   InterPro; IPR000878; 4pyrrol_Mease.
DR   InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR   InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR   InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR   InterPro; IPR006366; CobA/CysG_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR037115; Sirohaem_synt_dimer_dom_sf.
DR   InterPro; IPR012409; Sirohaem_synth.
DR   InterPro; IPR028281; Sirohaem_synthase_central.
DR   InterPro; IPR019478; Sirohaem_synthase_dimer_dom.
DR   InterPro; IPR006367; Sirohaem_synthase_N.
DR   InterPro; IPR003043; Uropor_MeTrfase_CS.
DR   Pfam; PF10414; CysG_dimeriser; 1.
DR   Pfam; PF14824; Sirohm_synth_M; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF036426; Sirohaem_synth; 2.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53790; SSF53790; 1.
DR   TIGRFAMs; TIGR01469; cobA_cysG_Cterm; 1.
DR   TIGRFAMs; TIGR01470; cysG_Nterm; 1.
DR   PROSITE; PS00840; SUMT_2; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01646,
KW   ECO:0000256|SAAS:SAAS01024974};
KW   Complete proteome {ECO:0000313|Proteomes:UP000247746};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01646,
KW   ECO:0000256|SAAS:SAAS01024979};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01646,
KW   ECO:0000256|RuleBase:RU003960, ECO:0000256|SAAS:SAAS00099290,
KW   ECO:0000313|EMBL:PYE38765.1};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01646,
KW   ECO:0000256|SAAS:SAAS01024984};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01646, ECO:0000256|SAAS:SAAS01024985};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01646,
KW   ECO:0000256|SAAS:SAAS01024988};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01646};
KW   Porphyrin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01646,
KW   ECO:0000256|SAAS:SAAS01024977};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01646,
KW   ECO:0000256|SAAS:SAAS00099242};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01646,
KW   ECO:0000256|RuleBase:RU003960, ECO:0000256|SAAS:SAAS00099286,
KW   ECO:0000313|EMBL:PYE38765.1}.
FT   DOMAIN      121    144       Sirohm_synth_M. {ECO:0000259|Pfam:
FT                                PF14824}.
FT   DOMAIN      150    207       CysG_dimeriser. {ECO:0000259|Pfam:
FT                                PF10414}.
FT   DOMAIN      247    455       TP_methylase. {ECO:0000259|Pfam:PF00590}.
FT   NP_BIND      22     23       NAD. {ECO:0000256|HAMAP-Rule:MF_01646}.
FT   NP_BIND      43     44       NAD. {ECO:0000256|HAMAP-Rule:MF_01646}.
FT   REGION        1    203       Precorrin-2 dehydrogenase /
FT                                sirohydrochlorin ferrochelatase.
FT                                {ECO:0000256|HAMAP-Rule:MF_01646}.
FT   REGION      245    545       Uroporphyrinogen-III C-methyltransferase.
FT                                {ECO:0000256|HAMAP-Rule:MF_01646}.
FT   REGION      330    332       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01646}.
FT   REGION      360    361       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01646}.
FT   ACT_SITE    277    277       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01646, ECO:0000256|PIRSR:PIRSR036426-
FT                                1}.
FT   ACT_SITE    299    299       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01646, ECO:0000256|PIRSR:PIRSR036426-
FT                                1}.
FT   BINDING     254    254       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01646}.
FT   BINDING     335    335       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01646}.
FT   BINDING     412    412       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01646}.
FT   BINDING     441    441       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01646}.
FT   MOD_RES     128    128       Phosphoserine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01646}.
SQ   SEQUENCE   545 AA;  59320 MW;  90DEDDB97F2090FE CRC64;
     MNTFPLFFKL EDRKVLIVGG GDVALRKADL LSRAGAAITI LAPVISDEIQ ALLNDSKHQL
     IYENYNNTYM SGARVIIAAT DDETLNHQIH ADATALNIPV NVVDTPHLCD FIFPAIVDRN
     PIVIGISSNG KAPVLARLLR ARLETLIPQG YGKLAKLAGE FRTEVKAKIP TLTGRRQFWE
     RAFEGKVSEL MFAGNEVQAT EQLQADLDST AANIASANES PTHTTVVAEP IVDNENSVEA
     NTPVGEVYIV GAGPGDPELL TFKALRLMQQ ADIVYYDALV SPQVLDLCRR DADKVFVGKK
     RSNHAVAQLG INELLVNSAK EGRRVVRLKG GDPFIFGRGG EEIESLRAHD IPYQVVPGIT
     AANAAASYAG IPLTHRDHSQ SVRFVTGFLK AGAPNSNFKS FLNTDETVVF YMGLHSLPRL
     TEGLIDAGRA DSTPIAIVSN ASMPNQQVLT GTLANIVELQ EQHQLPTPAL LIMGDVVALH
     DNLAWYNLQN QQHSQSSDDL AKNWLREGSR GKVEKQPIDQ QAHALSMISS LATQQEEGLE
     QLIID
//