(data stored in ACNUC7421 zone)

SWISSPROT: CYSG_PSEHT

ID   CYSG_PSEHT              Reviewed;         473 AA.
AC   Q3ILQ9;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 83.
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};
GN   OrderedLocusNames=PSHAa0213;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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:0000255|HAMAP-
CC       Rule:MF_01646}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uroporphyrinogen III
CC       = S-adenosyl-L-homocysteine + precorrin-1. {ECO:0000255|HAMAP-
CC       Rule:MF_01646}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + precorrin-1 = S-
CC       adenosyl-L-homocysteine + precorrin-2. {ECO:0000255|HAMAP-
CC       Rule:MF_01646}.
CC   -!- CATALYTIC ACTIVITY: Precorrin-2 + NAD(+) = sirohydrochlorin +
CC       NADH. {ECO:0000255|HAMAP-Rule:MF_01646}.
CC   -!- CATALYTIC ACTIVITY: Siroheme + 2 H(+) = sirohydrochlorin + Fe(2+).
CC       {ECO:0000255|HAMAP-Rule:MF_01646}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       precorrin-2 from uroporphyrinogen III: step 1/1.
CC       {ECO:0000255|HAMAP-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}.
DR   EMBL; CR954246; CAI85316.1; -; Genomic_DNA.
DR   RefSeq; WP_011326931.1; NC_007481.1.
DR   ProteinModelPortal; Q3ILQ9; -.
DR   SMR; Q3ILQ9; -.
DR   STRING; 326442.PSHAa0213; -.
DR   EnsemblBacteria; CAI85316; CAI85316; PSHAa0213.
DR   KEGG; pha:PSHAa0213; -.
DR   PATRIC; fig|326442.8.peg.204; -.
DR   eggNOG; ENOG4105CB8; Bacteria.
DR   eggNOG; COG0007; LUCA.
DR   eggNOG; COG1648; LUCA.
DR   HOGENOM; HOG000290518; -.
DR   KO; K02302; -.
DR   OMA; QVSEYWP; -.
DR   OrthoDB; POG091H0526; -.
DR   UniPathway; UPA00148; UER00211.
DR   UniPathway; UPA00148; UER00222.
DR   UniPathway; UPA00262; UER00211.
DR   UniPathway; UPA00262; UER00222.
DR   UniPathway; UPA00262; UER00376.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051266; F:sirohydrochlorin ferrochelatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019354; P:siroheme biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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;
DR   PRODOM; Q3ILQ9.
DR   SWISS-2DPAGE; Q3ILQ9.
KW   Cobalamin biosynthesis; Complete proteome; Lyase; Methyltransferase;
KW   Multifunctional enzyme; NAD; Oxidoreductase; Phosphoprotein;
KW   Porphyrin biosynthesis; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN         1    473       Siroheme synthase.
FT                                /FTId=PRO_0000330532.
FT   NP_BIND      22     23       NAD. {ECO:0000255|HAMAP-Rule:MF_01646}.
FT   NP_BIND      43     44       NAD. {ECO:0000255|HAMAP-Rule:MF_01646}.
FT   REGION        1    203       precorrin-2 dehydrogenase /
FT                                sirohydrochlorin ferrochelatase.
FT                                {ECO:0000255|HAMAP-Rule:MF_01646}.
FT   REGION      215    473       Uroporphyrinogen-III C-methyltransferase.
FT                                {ECO:0000255|HAMAP-Rule:MF_01646}.
FT   REGION      300    302       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01646}.
FT   REGION      330    331       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01646}.
FT   ACT_SITE    247    247       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01646}.
FT   ACT_SITE    269    269       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01646}.
FT   BINDING     224    224       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01646}.
FT   BINDING     305    305       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01646}.
FT   BINDING     382    382       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01646}.
FT   BINDING     411    411       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01646}.
FT   MOD_RES     128    128       Phosphoserine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01646}.
SQ   SEQUENCE   473 AA;  51809 MW;  64D87C039D7900D3 CRC64;
     MQYLPIFTKL DNKPVLVVGG GDVALRKCSA LLKARASITL VAPKFCQQLI ELASENKVTL
     IHEYFSEQHL KNMMLVIAAT DLEHVNSQVF ELANAHNIFV NVVDDQPKCT FIFPSIVDRN
     PITIAISSAG TAPVLARRLR EKLETLIPQH IGPLATLVGG FRSKVKQRFK HFADRRQFWE
     GVFDSSVVSK VQTGDTQAAE QQLEHMLNAK AEPEGEVYVV GAGPGDPELL TLKALQLMQQ
     ADVVVYDYLV SDEIMELVRR DADLICVGKR LGDHSVAQQD TNQMLVDLAK QGKKVCRIKG
     GDPFIYGRGG EEVQVLAANK VNYQIVPGIT AAAGCSAYAG IPLTHRDHAQ AIQFVTGHCK
     KDGQELDWQS LAKPNQTLAI YMGVIKSPHI QAELLKHGRN ANTPVAIIEN GTRKNQRVIT
     GKLGELADLI TRNSVVSPAL LIIGEVASLH QELHWFGAKA QTSSFAQPLT DVA
//

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