ID A0A351XP33_9GAMM Unreviewed; 462 AA. AC A0A351XP33; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 05-DEC-2018, entry version 2. 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=cobA {ECO:0000313|EMBL:HBA98464.1}; GN Synonyms=cysG {ECO:0000256|HAMAP-Rule:MF_01646}; GN ORFNames=DCY90_02605 {ECO:0000313|EMBL:HBA25256.1}, DCY92_01780 GN {ECO:0000313|EMBL:HBA28169.1}, DCY99_00760 GN {ECO:0000313|EMBL:HBA98464.1}, DD382_04285 GN {ECO:0000313|EMBL:HBN58491.1}, DD709_05225 GN {ECO:0000313|EMBL:HBQ24632.1}, DDW63_04190 GN {ECO:0000313|EMBL:HBG03696.1}, DEE99_00090 GN {ECO:0000313|EMBL:HBW06161.1}; OS Gammaproteobacteria bacterium. OC Bacteria; Proteobacteria; Gammaproteobacteria. OX NCBI_TaxID=1913989 {ECO:0000313|EMBL:HBA98464.1}; RN [1] {ECO:0000313|EMBL:HBA98464.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UBA10975 {ECO:0000313|EMBL:HBG03696.1}, UBA8250 RC {ECO:0000313|EMBL:HBA98464.1}, UBA8252 {ECO:0000313|EMBL:HBQ24632.1}, RC UBA8254 {ECO:0000313|EMBL:HBA28169.1}, UBA8255 RC {ECO:0000313|EMBL:HBA25256.1}, UBA8484 {ECO:0000313|EMBL:HBW06161.1}, RC and UBA9326 {ECO:0000313|EMBL:HBN58491.1}; RX PubMed=30148503; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny RT substantially revises the tree of life."; RL Nat. Biotechnol. 0:0-0(2018). 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:HBA98464.1}. 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; DNJK01000062; HBA25256.1; -; Genomic_DNA. DR EMBL; DNJI01000041; HBA28169.1; -; Genomic_DNA. DR EMBL; DNJS01000020; HBA98464.1; -; Genomic_DNA. DR EMBL; DNRK01000101; HBG03696.1; -; Genomic_DNA. DR EMBL; DOBR01000126; HBN58491.1; -; Genomic_DNA. DR EMBL; DOHH01000122; HBQ24632.1; -; Genomic_DNA. DR EMBL; DOPL01000004; HBW06161.1; -; Genomic_DNA. DR UniPathway; UPA00148; UER00222. DR UniPathway; UPA00262; UER00211. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. 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; 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}; 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:HBA98464.1}; 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:HBA98464.1}. FT DOMAIN 121 145 Sirohm_synth_M. {ECO:0000259|Pfam: FT PF14824}. FT DOMAIN 150 207 CysG_dimeriser. {ECO:0000259|Pfam: FT PF10414}. FT DOMAIN 218 427 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 216 462 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 383 383 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000256|HAMAP-Rule: FT MF_01646}. FT BINDING 412 412 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 462 AA; 50397 MW; 82D08BA0DC3DB415 CRC64; MNYLPIFIDI TQQPCLVVGG GDIALRKINL LLKANAAVTC VSKECCNGIE KLVKDNKIIR IEKAFEATDI NAQVLIVSAT DDSDLNAQVS ALAKTANIPV NVVDSPDLCS FVMPSIVDRS PIVIAISSAG KAPVLARLIR AKLESTIPHA YGKLAELAGN FRDQVKAKFN NIEDRRYFWE KTFSGIVAEK VFSGKVDEAK ADLQAQLDGS TDSGIGEVYL VGGGPGDPDL LTFKALRLMQ QADVILYDRL VSDGVMELVR RDAELIYVGK ERDNHAVPQG DINQLLVDLA KQGRRVCRLK GGDPFIFGRG GEEIETLAEN NIPFQVVPGI TAASGCSAYS GIPLTHRDYS QSCRFVTGHL KDGSMNLPWD ELAVEQQTIV FYMALVGARH LSEQLISHGM RGDMPVALVE KGTTPDHQVY VTTLAELPNL VENTTIHAPT LIIIGEVVKL REKLNWFDAD ND //