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Database: UniProt
Entry: U3AKJ0_9VIBR
LinkDB: U3AKJ0_9VIBR
Original site: U3AKJ0_9VIBR 
ID   U3AKJ0_9VIBR            Unreviewed;       311 AA.
AC   U3AKJ0;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Porphobilinogen deaminase {ECO:0000256|HAMAP-Rule:MF_00260};
DE            Short=PBG {ECO:0000256|HAMAP-Rule:MF_00260};
DE            EC=2.5.1.61 {ECO:0000256|HAMAP-Rule:MF_00260};
DE   AltName: Full=Hydroxymethylbilane synthase {ECO:0000256|HAMAP-Rule:MF_00260};
DE            Short=HMBS {ECO:0000256|HAMAP-Rule:MF_00260};
DE   AltName: Full=Pre-uroporphyrinogen synthase {ECO:0000256|HAMAP-Rule:MF_00260};
GN   Name=hemC {ECO:0000256|HAMAP-Rule:MF_00260,
GN   ECO:0000313|EMBL:GAD80441.1};
GN   ORFNames=VEZ01S_37_00060 {ECO:0000313|EMBL:GAD80441.1};
OS   Vibrio ezurae NBRC 102218.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1219080 {ECO:0000313|EMBL:GAD80441.1, ECO:0000313|Proteomes:UP000016562};
RN   [1] {ECO:0000313|EMBL:GAD80441.1, ECO:0000313|Proteomes:UP000016562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 102218 {ECO:0000313|EMBL:GAD80441.1,
RC   ECO:0000313|Proteomes:UP000016562};
RA   Yoshida I., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y.,
RA   Tsuchikane K., Noguchi M., Hirakata S., Ichikawa N., Ohji S., Yamazoe A.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Vibrio ezurae NBRC 102218.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Tetrapolymerization of the monopyrrole PBG into the
CC       hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
CC       {ECO:0000256|ARBA:ARBA00002869, ECO:0000256|HAMAP-Rule:MF_00260}.
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         Evidence={ECO:0000256|ARBA:ARBA00000416, ECO:0000256|HAMAP-
CC         Rule:MF_00260};
CC   -!- COFACTOR:
CC       Name=dipyrromethane; Xref=ChEBI:CHEBI:60342;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00260};
CC       Note=Binds 1 dipyrromethane group covalently. {ECO:0000256|HAMAP-
CC       Rule:MF_00260};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
CC       {ECO:0000256|ARBA:ARBA00004735}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC       Rule:MF_00260}.
CC   -!- MISCELLANEOUS: The porphobilinogen subunits are added to the
CC       dipyrromethane group. {ECO:0000256|HAMAP-Rule:MF_00260}.
CC   -!- SIMILARITY: Belongs to the HMBS family. {ECO:0000256|ARBA:ARBA00005638,
CC       ECO:0000256|HAMAP-Rule:MF_00260}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAD80441.1}.
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DR   EMBL; BATM01000037; GAD80441.1; -; Genomic_DNA.
DR   RefSeq; WP_021714149.1; NZ_BATM01000037.1.
DR   AlphaFoldDB; U3AKJ0; -.
DR   STRING; 1219080.VEZ01S_37_00060; -.
DR   eggNOG; COG0181; Bacteria.
DR   OrthoDB; 9810298at2; -.
DR   UniPathway; UPA00251; UER00319.
DR   Proteomes; UP000016562; Unassembled WGS sequence.
DR   GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd13646; PBP2_EcHMBS_like; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   Gene3D; 3.30.160.40; Porphobilinogen deaminase, C-terminal domain; 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   NCBIfam; TIGR00212; hemC; 1.
DR   PANTHER; PTHR11557; PORPHOBILINOGEN DEAMINASE; 1.
DR   PANTHER; PTHR11557:SF0; PORPHOBILINOGEN DEAMINASE; 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; SSF53850; Periplasmic binding protein-like II; 1.
DR   SUPFAM; SSF54782; Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain; 1.
DR   PROSITE; PS00533; PORPHOBILINOGEN_DEAM; 1.
PE   3: Inferred from homology;
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP-
KW   Rule:MF_00260}; Reference proteome {ECO:0000313|Proteomes:UP000016562};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00260}.
FT   DOMAIN          6..213
FT                   /note="Porphobilinogen deaminase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01379"
FT   DOMAIN          227..297
FT                   /note="Porphobilinogen deaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03900"
FT   MOD_RES         242
FT                   /note="S-(dipyrrolylmethanemethyl)cysteine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00260"
SQ   SEQUENCE   311 AA;  34044 MW;  FFF051DB22480F4A CRC64;
     MSKQTLRIAT RKSPLALWQA HYVKSRLEEI HPDLDIELVT MVTKGDIILD TPLAKVGGKG
     LFVKELEVAM LEERADIAVH SMKDVPVDFP QGLGLAVICE REDPRDAFVS NTYHSIDELP
     HGATVGTCSL RRQCQISAAR PDIIIKELRG NVGTRLGKLD DGQYDAIILA AAGLKRLKLE
     ERIQSYIEPE QSLPAVGQGA VGIECRVDDQ RVLDLIQPLN DPDTSDRVLA ERAMNLALEG
     GCQVPIGSYC VITPDNKLHL RGLVGKPDGT KIIRAESVSE RSQAIKMGEE LAQQLLNLGA
     KEILSDVYSQ G
//
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