ID   A0A2V4VIV6_9GAMM        Unreviewed;       545 AA.
AC   A0A2V4VIV6;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   29-SEP-2021, entry version 16.
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=SUMT {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   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};
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};
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 genomes of
RT   soil and plant-associated and newly described type 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 form
CC       precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring
CC       dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it
CC       catalyzes the ferrochelation of sirohydrochlorin to yield siroheme.
CC       {ECO:0000256|HAMAP-Rule:MF_01646}.
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   -!- 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   -!- 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; EC=1.3.1.76;
CC         Evidence={ECO:0000256|ARBA:ARBA00001156, ECO:0000256|HAMAP-
CC         Rule:MF_01646};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       precorrin-2 from uroporphyrinogen III: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01646}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       sirohydrochlorin from precorrin-2: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01646}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC       biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005010, ECO:0000256|HAMAP-Rule:MF_01646}.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005879, 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   -!- SIMILARITY: In the N-terminal section; belongs to the precorrin-2
CC       dehydrogenase / sirohydrochlorin ferrochelatase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01646}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PYE38765.1}.
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DR   EMBL; QJSU01000006; PYE38765.1; -; Genomic_DNA.
DR   EnsemblBacteria; PYE38765; PYE38765; DFP82_106170.
DR   UniPathway; UPA00148; UER00211.
DR   UniPathway; UPA00262; UER00222.
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:0032259; P:methylation; IEA:UniProtKB-KW.
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|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW   Rule:MF_01646};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01646};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_01646};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW   Rule:MF_01646};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01646};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01646};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW   Rule:MF_01646};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP-
KW   Rule:MF_01646};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01646};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01646}.
FT   DOMAIN          121..144
FT                   /note="Sirohm_synth_M"
FT                   /evidence="ECO:0000259|Pfam:PF14824"
FT   DOMAIN          150..207
FT                   /note="CysG_dimeriser"
FT                   /evidence="ECO:0000259|Pfam:PF10414"
FT   DOMAIN          247..455
FT                   /note="TP_methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
FT   NP_BIND         22..23
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646"
FT   NP_BIND         43..44
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646"
FT   REGION          1..203
FT                   /note="Precorrin-2 dehydrogenase / sirohydrochlorin
FT                   ferrochelatase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646"
FT   REGION          245..545
FT                   /note="Uroporphyrinogen-III C-methyltransferase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646"
FT   REGION          330..332
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646"
FT   REGION          360..361
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646"
FT   ACT_SITE        277
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646,
FT                   ECO:0000256|PIRSR:PIRSR036426-1"
FT   ACT_SITE        299
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646,
FT                   ECO:0000256|PIRSR:PIRSR036426-1"
FT   BINDING         254
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646"
FT   BINDING         335
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646"
FT   BINDING         412
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646"
FT   BINDING         441
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen and
FT                   carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646"
FT   MOD_RES         128
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000256|HAMAP-Rule: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
//