ID A0A066ZYM1_HYDMR Unreviewed; 484 AA. AC A0A066ZYM1; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 05-JUN-2019, entry version 45. 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=EI16_03910 {ECO:0000313|EMBL:KDN95456.1}; OS Hydrogenovibrio marinus. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Hydrogenovibrio. OX NCBI_TaxID=28885 {ECO:0000313|EMBL:KDN95456.1, ECO:0000313|Proteomes:UP000027341}; RN [1] {ECO:0000313|EMBL:KDN95456.1, ECO:0000313|Proteomes:UP000027341} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MH-110 {ECO:0000313|EMBL:KDN95456.1, RC ECO:0000313|Proteomes:UP000027341}; RA Cha H.J., Jo B.H., Hwang B.H.; RT "Draft genome sequence of Hydrogenovibrio marinus MH-110, a model RT organism for aerobic H2 metabolism."; RL Submitted (APR-2014) 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:SAAS01123671}; 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:SAAS01116480}; 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:SAAS01123666}; 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: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01646}. 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:KDN95456.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JMIU01000001; KDN95456.1; -; Genomic_DNA. DR EnsemblBacteria; KDN95456; KDN95456; EI16_03910. DR UniPathway; UPA00148; UER00222. DR UniPathway; UPA00262; UER00211. DR Proteomes; UP000027341; 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; 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; 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; 1. 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}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000027341}; 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:SAAS00467449}; 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 Porphyrin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01646, KW ECO:0000256|SAAS:SAAS01024977}; KW Reference proteome {ECO:0000313|Proteomes:UP000027341}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01646, KW ECO:0000256|SAAS:SAAS00467481}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01646, KW ECO:0000256|RuleBase:RU003960, ECO:0000256|SAAS:SAAS00467429}. FT DOMAIN 127 151 Sirohm_synth_M. {ECO:0000259|Pfam: FT PF14824}. FT DOMAIN 157 213 CysG_dimeriser. {ECO:0000259|Pfam: FT PF10414}. FT DOMAIN 227 436 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 1 209 Precorrin-2 dehydrogenase / FT sirohydrochlorin ferrochelatase. FT {ECO:0000256|HAMAP-Rule:MF_01646}. FT REGION 225 484 Uroporphyrinogen-III C-methyltransferase. FT {ECO:0000256|HAMAP-Rule:MF_01646}. FT REGION 310 312 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_01646}. FT REGION 340 341 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_01646}. FT COILED 456 476 {ECO:0000256|SAM:Coils}. FT ACT_SITE 257 257 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01646, ECO:0000256|PIRSR:PIRSR036426- FT 1}. FT ACT_SITE 279 279 Proton donor. {ECO:0000256|HAMAP-Rule: FT MF_01646, ECO:0000256|PIRSR:PIRSR036426- FT 1}. FT BINDING 234 234 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_01646}. FT BINDING 315 315 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_01646}. FT BINDING 392 392 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000256|HAMAP-Rule: FT MF_01646}. FT BINDING 421 421 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01646}. SQ SEQUENCE 484 AA; 52445 MW; DB4658D4EE804930 CRC64; MDYLPIFMNI KQQACLIVGG GVVAARKADL FIQSGAQVMV IAPALKSEMQ SFLNQNKVTW HQGVFSPKVM ADVFGEQLPK LVISATDNQA VNIAVYEYCQ AAGIPVNVAD QTEYCDFILP AIVDRAPMTI AISTGGRSPV LARVMKAKLE TMIPHGFGRL TDLVGRYRDK VKAAISSIDG RKAFWESLLD GLFIDKAVHG LDGEAEALLE KKLEQADNFE EAAVGEVYVI GAGPGDPELM TFKAQRLLQQ ADVVLYDRLV SPEIVDMARR EAERVYVGKK SKHHAVPQED ICRMLVEYAK QGKKVARLKG GDPYIFGRGG EEVEILAKAG VAYQVVPGIT AAAGCAAYAD FPLTHREFSQ SVALVTGHQQ EGGNAIDYGR LAHSGDTMVF YMGIKNAPKI QAGLIAHGMN PGTPAAIIER GTRADQKVTV SSLGKLTETI AKQAIKPPAL LVVGEVVKVR ERIQNAKRFV QQAEQSPPLH RVAV //