HEM3_VIBCH
ID HEM3_VIBCH Reviewed; 311 AA.
AC Q9KVM1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Porphobilinogen deaminase;
DE Short=PBG;
DE EC=2.5.1.61;
DE AltName: Full=Hydroxymethylbilane synthase;
DE Short=HMBS;
DE AltName: Full=Pre-uroporphyrinogen synthase;
GN Name=hemC; OrderedLocusNames=VC_0120;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF93298.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE003852; AAF93298.1; ALT_INIT; Genomic_DNA.
DR PIR; F82362; F82362.
DR RefSeq; NP_229779.1; NC_002505.1.
DR RefSeq; WP_000141022.1; NZ_LT906614.1.
DR PDB; 5H6O; X-ray; 2.70 A; A=1-311.
DR PDBsum; 5H6O; -.
DR AlphaFoldDB; Q9KVM1; -.
DR SMR; Q9KVM1; -.
DR STRING; 243277.VC_0120; -.
DR PRIDE; Q9KVM1; -.
DR DNASU; 2614463; -.
DR EnsemblBacteria; AAF93298; AAF93298; VC_0120.
DR GeneID; 57741382; -.
DR KEGG; vch:VC_0120; -.
DR PATRIC; fig|243277.26.peg.111; -.
DR eggNOG; COG0181; Bacteria.
DR HOGENOM; CLU_019704_0_2_6; -.
DR OMA; LWQANHI; -.
DR UniPathway; UPA00251; UER00319.
DR Proteomes; UP000000584; Chromosome 1.
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 1: Evidence at protein level;
KW 3D-structure; Porphyrin biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..311
FT /note="Porphobilinogen deaminase"
FT /id="PRO_0000143005"
FT MOD_RES 242
FT /note="S-(dipyrrolylmethanemethyl)cysteine"
FT /evidence="ECO:0000250"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:5H6O"
FT HELIX 14..30
FT /evidence="ECO:0007829|PDB:5H6O"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:5H6O"
FT HELIX 64..71
FT /evidence="ECO:0007829|PDB:5H6O"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:5H6O"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:5H6O"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:5H6O"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:5H6O"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:5H6O"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:5H6O"
FT HELIX 130..139
FT /evidence="ECO:0007829|PDB:5H6O"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:5H6O"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:5H6O"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:5H6O"
FT HELIX 171..176
FT /evidence="ECO:0007829|PDB:5H6O"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:5H6O"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:5H6O"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:5H6O"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:5H6O"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:5H6O"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:5H6O"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:5H6O"
FT HELIX 222..238
FT /evidence="ECO:0007829|PDB:5H6O"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:5H6O"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:5H6O"
FT STRAND 256..264
FT /evidence="ECO:0007829|PDB:5H6O"
FT STRAND 271..278
FT /evidence="ECO:0007829|PDB:5H6O"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:5H6O"
FT HELIX 283..295
FT /evidence="ECO:0007829|PDB:5H6O"
FT TURN 296..299
FT /evidence="ECO:0007829|PDB:5H6O"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:5H6O"
SQ SEQUENCE 311 AA; 33849 MW; 1EB05C0791FC62AD CRC64;
MTETPIRIAT RQSPLALWQA NYVKDALMAA HPGLQVELVT MVTRGDVILD TPLAKVGGKG
LFVKELEIAM LEGRADLAVH SMKDVPVDFP DGLGLVTICE REDPRDAFVS NTYAKIEDLP
SGAIVGTCSL RRQCQLKAAR PDLVIKELRG NVGTRLSKLD AGEYDAIILA AAGLKRLELE
SRIRSFIEPE QSLPAVGQGA VGIECRVNDQ RVRALLAPLN HADTADRVRC ERAMNLTLQG
GCQVPIGSYA LLEGDTIWLR ALVGEPDGSQ IVRGEIRGPR TQAEQLGITL AEQLLSQGAK
EILERLYCDH E
