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HEM31_STRCO
ID   HEM31_STRCO             Reviewed;         319 AA.
AC   Q9WX16;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=Porphobilinogen deaminase 1;
DE            Short=PBG 1;
DE            EC=2.5.1.61;
DE   AltName: Full=Hydroxymethylbilane synthase 1;
DE            Short=HMBS 1;
DE   AltName: Full=Pre-uroporphyrinogen synthase 1;
GN   Name=hemC1; OrderedLocusNames=SCO3318; ORFNames=SCE68.16c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: Tetrapolymerization of the monopyrrole PBG into the
CC       hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+);
CC         Xref=Rhea:RHEA:13185, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57845, ChEBI:CHEBI:58126; EC=2.5.1.61;
CC   -!- COFACTOR:
CC       Name=dipyrromethane; Xref=ChEBI:CHEBI:60342; Evidence={ECO:0000250};
CC       Note=Binds 1 dipyrromethane group covalently. {ECO:0000250};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: The porphobilinogen subunits are added to the
CC       dipyrromethane group. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HMBS family. {ECO:0000305}.
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DR   EMBL; AL939116; CAB45352.1; -; Genomic_DNA.
DR   PIR; T36266; T36266.
DR   RefSeq; NP_627528.1; NC_003888.3.
DR   RefSeq; WP_003975518.1; NZ_VNID01000025.1.
DR   AlphaFoldDB; Q9WX16; -.
DR   SMR; Q9WX16; -.
DR   STRING; 100226.SCO3318; -.
DR   GeneID; 1098752; -.
DR   KEGG; sco:SCO3318; -.
DR   PATRIC; fig|100226.15.peg.3378; -.
DR   eggNOG; COG0181; Bacteria.
DR   HOGENOM; CLU_019704_1_0_11; -.
DR   InParanoid; Q9WX16; -.
DR   OMA; LWQANHI; -.
DR   PhylomeDB; Q9WX16; -.
DR   UniPathway; UPA00251; UER00319.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004418; F:hydroxymethylbilane synthase activity; IBA:GO_Central.
DR   GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
DR   GO; GO:0018160; P:peptidyl-pyrromethane cofactor linkage; IEA:InterPro.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.160.40; -; 1.
DR   HAMAP; MF_00260; Porphobil_deam; 1.
DR   InterPro; IPR000860; HemC.
DR   InterPro; IPR022419; Porphobilin_deaminase_cofac_BS.
DR   InterPro; IPR022417; Porphobilin_deaminase_N.
DR   InterPro; IPR022418; Porphobilinogen_deaminase_C.
DR   InterPro; IPR036803; Porphobilinogen_deaminase_C_sf.
DR   PANTHER; PTHR11557; PTHR11557; 1.
DR   Pfam; PF01379; Porphobil_deam; 1.
DR   Pfam; PF03900; Porphobil_deamC; 1.
DR   PIRSF; PIRSF001438; 4pyrrol_synth_OHMeBilane_synth; 1.
DR   PRINTS; PR00151; PORPHBDMNASE.
DR   SUPFAM; SSF54782; SSF54782; 1.
DR   TIGRFAMs; TIGR00212; hemC; 1.
DR   PROSITE; PS00533; PORPHOBILINOGEN_DEAM; 1.
PE   3: Inferred from homology;
KW   Porphyrin biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..319
FT                   /note="Porphobilinogen deaminase 1"
FT                   /id="PRO_0000142999"
FT   MOD_RES         244
FT                   /note="S-(dipyrrolylmethanemethyl)cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   319 AA;  33137 MW;  538D6BCCFAD53012 CRC64;
     MTEKALRLGT RRSKLAMAQS GQVADAVSQV TGRPVELVEI TTYGDTSREH LAQIGGTGVF
     VAALRDALLR GEVDFAVHSL KDLPTAQHEG LVVAAIPERE DPRDVVVARD ARKLTDLPRG
     ARVGTGAPRR MAQLNAYART HGMEIETVPI RGNVDTRIGY VRSGELDAVV LAAAGLNRVG
     RIDEVTDFLS VDTVLPAPGQ GALAVECAAD NASLIAALAE LDDPFTRAAV TAERSLLAAL
     EAGCSAPVGA LADLLADGQT VKEMRLRGVV GTTDGSTLVQ LSTTGPVPET HEAALALGGE
     LAAEMLAQGA AGLMGERAQ
 
 
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