ID A0A2V4VIV6_9GAMM Unreviewed; 545 AA. AC A0A2V4VIV6; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 24-JAN-2024, entry version 25. 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; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC 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; precorrin-2 from uroporphyrinogen III: step 1/1. CC {ECO:0000256|ARBA:ARBA00025705, ECO:0000256|HAMAP-Rule:MF_01646}. CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme CC biosynthesis; siroheme from sirohydrochlorin: step 1/1. CC {ECO:0000256|HAMAP-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}. 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; QJSU01000006; PYE38765.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2V4VIV6; -. DR OrthoDB; 9815856at2; -. DR UniPathway; UPA00148; UER00211. 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:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0019354; P:siroheme biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd11642; SUMT; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR Gene3D; 1.10.8.210; Sirohaem synthase, dimerisation domain; 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 NCBIfam; TIGR01469; cobA_cysG_Cterm; 1. DR NCBIfam; TIGR01470; cysG_Nterm; 1. DR PANTHER; PTHR45790:SF1; SIROHEME SYNTHASE; 1. DR PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1. DR Pfam; PF10414; CysG_dimeriser; 1. DR Pfam; PF13241; NAD_binding_7; 1. DR Pfam; PF14824; Sirohm_synth_M; 1. DR Pfam; PF00590; TP_methylase; 1. DR PIRSF; PIRSF036426; Sirohaem_synth; 2. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR SUPFAM; SSF75615; Siroheme synthase middle domains-like; 1. DR SUPFAM; SSF53790; Tetrapyrrole methylase; 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}; Phosphoprotein {ECO:0000256|HAMAP-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="Siroheme synthase central" FT /evidence="ECO:0000259|Pfam:PF14824" FT DOMAIN 150..206 FT /note="Sirohaem synthase dimerisation" FT /evidence="ECO:0000259|Pfam:PF10414" FT DOMAIN 247..456 FT /note="Tetrapyrrole methylase" FT /evidence="ECO:0000259|Pfam:PF00590" 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 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 22..23 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT BINDING 43..44 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT BINDING 254 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT BINDING 330..332 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT BINDING 335 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT BINDING 360..361 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT BINDING 412 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT BINDING 441 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" 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 //