ID A0A0T9XSH3_SALET Unreviewed; 457 AA. AC A0A0T9XSH3; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 16-MAR-2016, entry version 2. DE RecName: Full=Siroheme synthase {ECO:0000256|HAMAP-Rule:MF_01646}; GN Name=cysG {ECO:0000256|HAMAP-Rule:MF_01646, GN ECO:0000313|EMBL:CNU86473.1}; GN ORFNames=ERS008202_03718 {ECO:0000313|EMBL:CNU86473.1}, GN ERS008207_04139 {ECO:0000313|EMBL:CNV04810.1}, ERS008210_01062 GN {ECO:0000313|EMBL:CPR44771.1}, ERS008215_02382 GN {ECO:0000313|EMBL:CFW73352.1}; OS Salmonella enterica subsp. enterica serovar Bovismorbificans. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=58097 {ECO:0000313|EMBL:CNU86473.1, ECO:0000313|Proteomes:UP000039541}; RN [1] {ECO:0000313|EMBL:CNU86473.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3476 {ECO:0000313|EMBL:CNU86473.1}, 51892776 RC {ECO:0000313|EMBL:CPR44771.1}, A31126 {ECO:0000313|EMBL:CFW73352.1}, RC and D4891 {ECO:0000313|EMBL:CNV04810.1}; RA Murphy D.; RL Submitted (MAR-2015) 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:SAAS00025908}. CC -!- CATALYTIC ACTIVITY: Precorrin-2 + NAD(+) = sirohydrochlorin + CC NADH. {ECO:0000256|HAMAP-Rule:MF_01646, CC ECO:0000256|SAAS:SAAS00026054}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + precorrin-1 = S- CC adenosyl-L-homocysteine + precorrin-2. {ECO:0000256|HAMAP- CC Rule:MF_01646, ECO:0000256|SAAS:SAAS00227440}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uroporphyrinogen III CC = S-adenosyl-L-homocysteine + precorrin-1. {ECO:0000256|HAMAP- CC Rule:MF_01646, ECO:0000256|SAAS:SAAS00227483}. CC -!- CATALYTIC ACTIVITY: Siroheme + 2 H(+) = sirohydrochlorin + Fe(2+). CC {ECO:0000256|HAMAP-Rule:MF_01646, ECO:0000256|SAAS:SAAS00025860}. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC precorrin-2 from uroporphyrinogen III: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_01646, ECO:0000256|SAAS:SAAS00025958}. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC sirohydrochlorin from precorrin-2: step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_01646, ECO:0000256|SAAS:SAAS00025945}. 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:SAAS00025967}. 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:SAAS00025931}. 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:SAAS00025893}. 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 -!- SIMILARITY: In the N-terminal section; belongs to the precorrin-2 CC dehydrogenase / sirohydrochlorin ferrochelatase family. CC {ECO:0000256|HAMAP-Rule:MF_01646}. 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; CGIA01000007; CFW73352.1; -; Genomic_DNA. DR EMBL; CQPC01000062; CNU86473.1; -; Genomic_DNA. DR EMBL; CQPD01000056; CNV04810.1; -; Genomic_DNA. DR EMBL; CSTI01000004; CPR44771.1; -; Genomic_DNA. DR RefSeq; WP_000349896.1; NZ_CSTH01000032.1. DR UniPathway; UPA00148; UER00211. DR UniPathway; UPA00262; UER00211. DR Proteomes; UP000039385; Unassembled WGS sequence. DR Proteomes; UP000039541; Unassembled WGS sequence. DR Proteomes; UP000042394; Unassembled WGS sequence. DR Proteomes; UP000048853; Unassembled WGS sequence. DR Gene3D; 1.10.8.210; -; 1. DR Gene3D; 3.30.950.10; -; 1. DR Gene3D; 3.40.1010.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_01646; Siroheme_synth; 1. DR InterPro; IPR000878; 4pyrrol_Mease. DR InterPro; IPR014777; 4pyrrole_Mease_sub1. DR InterPro; IPR014776; 4pyrrole_Mease_sub2. DR InterPro; IPR006366; CobA/CysG_C. DR InterPro; IPR016040; NAD(P)-bd_dom. 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; PF13241; NAD_binding_7; 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; PS00839; SUMT_1; 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:SAAS00428831}; KW Complete proteome {ECO:0000313|Proteomes:UP000039385, KW ECO:0000313|Proteomes:UP000039541, ECO:0000313|Proteomes:UP000042394, KW ECO:0000313|Proteomes:UP000048853}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01646, KW ECO:0000256|SAAS:SAAS00428804}; 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:SAAS00428961}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01646, ECO:0000256|SAAS:SAAS00428848}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01646, KW ECO:0000256|SAAS:SAAS00428906, ECO:0000313|EMBL:CNU86473.1}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01646}; KW Porphyrin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01646, KW ECO:0000256|SAAS:SAAS00438752}; 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 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 1 204 precorrin-2 dehydrogenase / FT sirohydrochlorin ferrochelatase. FT {ECO:0000256|HAMAP-Rule:MF_01646}. FT REGION 216 457 Uroporphyrinogen-III C-methyltransferase. FT {ECO:0000256|HAMAP-Rule:MF_01646}. FT REGION 301 303 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_01646}. FT REGION 331 332 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_01646}. FT ACT_SITE 248 248 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01646}. FT ACT_SITE 270 270 Proton donor. {ECO:0000256|HAMAP-Rule: FT MF_01646}. FT BINDING 225 225 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_01646}. FT BINDING 306 306 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_01646}. FT BINDING 382 382 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000256|HAMAP-Rule: FT MF_01646}. FT BINDING 411 411 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 457 AA; 50133 MW; 359C8CA8D578092D CRC64; MDHLPIFCQL RDRDCLIVGG GDVAERKARL LLEAGARLTV NALTFIPQFT VWANEGMLTL VEGPFDETLL DSCWLAIAAT DDDTVNQRVS DAAESRRIFC NVVDAPKAAS FIMPSIIDRS PLMVAVSSGG TSPVLARLLR EKLESLLPQH LGQVARYAGQ LRARVKKQFA TMGERRRFWE KFFVNDRLAQ SLANADEKAV NATTERLFSE PLDHRGEVVL VGAGPGDAGL LTLKGLQQIQ QADIVVYDRL VSDDIMNLVR RDADRVFVGK RAGYHCVPQE EINQILLREA QKGKRVVRLK GGDPFIFGRG GEELETLCHA GIPFSVVPGI TAASGCSAYS GIPLTHRDYA QSVRLVTGHL KTGGELDWEN LAAEKQTLVF YMGLNQAATI QEKLIAFGMQ ADMPVALVEN GTSVKQRVVH GVLTQLGELA QQVESPALII VGRVVGLRDK LNWFSNH //