CYSG_PSYA2
ID CYSG_PSYA2 Reviewed; 549 AA.
AC Q4FSU1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Siroheme synthase {ECO:0000255|HAMAP-Rule:MF_01646};
DE Includes:
DE RecName: Full=Uroporphyrinogen-III C-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01646};
DE Short=Urogen III methylase {ECO:0000255|HAMAP-Rule:MF_01646};
DE EC=2.1.1.107 {ECO:0000255|HAMAP-Rule:MF_01646};
DE AltName: Full=SUMT {ECO:0000255|HAMAP-Rule:MF_01646};
DE AltName: Full=Uroporphyrinogen III methylase {ECO:0000255|HAMAP-Rule:MF_01646};
DE Short=UROM {ECO:0000255|HAMAP-Rule:MF_01646};
DE Includes:
DE RecName: Full=Precorrin-2 dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01646};
DE EC=1.3.1.76 {ECO:0000255|HAMAP-Rule:MF_01646};
DE Includes:
DE RecName: Full=Sirohydrochlorin ferrochelatase {ECO:0000255|HAMAP-Rule:MF_01646};
DE EC=4.99.1.4 {ECO:0000255|HAMAP-Rule:MF_01646};
GN Name=cysG {ECO:0000255|HAMAP-Rule:MF_01646}; OrderedLocusNames=Psyc_1065;
OS Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=259536;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17307 / VKM B-2377 / 273-4;
RX PubMed=20154119; DOI=10.1128/aem.02101-09;
RA Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA Murray A., Thomashow M., Tiedje J.M.;
RT "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT temperature growth.";
RL Appl. Environ. Microbiol. 76:2304-2312(2010).
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:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01646};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC precorrin-2 from uroporphyrinogen III: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01646}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC sirohydrochlorin from precorrin-2: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01646}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_01646}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC biosynthesis; siroheme from sirohydrochlorin: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_01646}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_01646}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the precorrin-2
CC dehydrogenase / sirohydrochlorin ferrochelatase family.
CC {ECO:0000255|HAMAP-Rule:MF_01646}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the precorrin
CC methyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01646}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAZ18917.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000082; AAZ18917.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041757642.1; NC_007204.1.
DR AlphaFoldDB; Q4FSU1; -.
DR SMR; Q4FSU1; -.
DR STRING; 259536.Psyc_1065; -.
DR EnsemblBacteria; AAZ18917; AAZ18917; Psyc_1065.
DR KEGG; par:Psyc_1065; -.
DR eggNOG; COG0007; Bacteria.
DR eggNOG; COG1648; Bacteria.
DR HOGENOM; CLU_011276_2_1_6; -.
DR OMA; KMTVVVY; -.
DR OrthoDB; 1185397at2; -.
DR UniPathway; UPA00148; UER00211.
DR UniPathway; UPA00148; UER00222.
DR UniPathway; UPA00262; UER00211.
DR UniPathway; UPA00262; UER00222.
DR UniPathway; UPA00262; UER00376.
DR Proteomes; UP000000546; Chromosome.
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 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; Lyase; Methyltransferase; Multifunctional enzyme;
KW NAD; Oxidoreductase; Phosphoprotein; Porphyrin biosynthesis;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..549
FT /note="Siroheme synthase"
FT /id="PRO_0000330546"
FT REGION 1..203
FT /note="Precorrin-2 dehydrogenase /sirohydrochlorin
FT ferrochelatase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT REGION 247..549
FT /note="Uroporphyrinogen-III C-methyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT ACT_SITE 279
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT ACT_SITE 301
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT BINDING 22..23
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT BINDING 43..44
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT BINDING 256
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT BINDING 332..334
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT BINDING 337
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT BINDING 362..363
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT BINDING 414
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT BINDING 443
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
SQ SEQUENCE 549 AA; 59727 MW; 019AACCDA20937C4 CRC64;
MNTFPLFFKL EDRKVLIVGG GDVALRKADL LSRAGACITV LAPSINHEIQ ALLSSSKHEL
IYEHYNKTYM TNSRVIIAAT DDERLNHQIH ADATALNIPV NVVDTPHLCD FIFPAIVDRN
PIVIGISSNG KAPVLARLLR ARLETLIPQG YGKLAKLAGE FRGDVKAKIP TLTGRRQFWE
RAFEGKVSQL MFAGNENEAL AQLQADLDNT AASITAKDAT DDNGLSTAST SAPAIANEFT
AARNTMGEVY IVGAGPGDPE LLTFKALRLM QQADIVYYDA LVSPQVLDLC RRDADKVFVG
KKRRNHAVAQ LGINELLVNS AKEGRRVVRL KGGDPFIFGR GGEEIESLRA HNIPYQVVPG
ITAANAAASY AGIPLTHRDH SQSVRFVTGF LKAGAPNNNF KNFLDTDETV VFYMGLHSLP
RLTEGLIDAG RSAETPIAIV SNASMPNQQV LTGTLASIVE LQEKNQLPTP ALLIMGDVVS
LHHDLAWYNL HNQQHNQNTS ETDNNWLRGG TATTPKSNAQ FNAHQQAHAL SMITNLATED
GDLEQLIIG
