ID A0A1S1JAN9_9FLAO Unreviewed; 307 AA.
AC A0A1S1JAN9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=hydroxymethylbilane synthase {ECO:0000256|ARBA:ARBA00012655};
DE EC=2.5.1.61 {ECO:0000256|ARBA:ARBA00012655};
GN ORFNames=BHE19_03470 {ECO:0000313|EMBL:OHT46579.1};
OS Flavobacterium tructae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1114873 {ECO:0000313|EMBL:OHT46579.1, ECO:0000313|Proteomes:UP000180252};
RN [1] {ECO:0000313|Proteomes:UP000180252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSU {ECO:0000313|Proteomes:UP000180252};
RA Chen S., Walker E.;
RL Submitted (SEP-2016) 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}.
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};
CC -!- COFACTOR:
CC Name=dipyrromethane; Xref=ChEBI:CHEBI:60342;
CC Evidence={ECO:0000256|ARBA:ARBA00001916};
CC -!- SIMILARITY: Belongs to the HMBS family.
CC {ECO:0000256|ARBA:ARBA00005638}.
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:OHT46579.1}.
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DR EMBL; MIKE01000011; OHT46579.1; -; Genomic_DNA.
DR RefSeq; WP_070906283.1; NZ_MUHG01000005.1.
DR AlphaFoldDB; A0A1S1JAN9; -.
DR STRING; 1278819.BHE19_03470; -.
DR OrthoDB; 9810298at2; -.
DR Proteomes; UP000180252; Unassembled WGS sequence.
DR GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd13647; PBP2_PBGD_2; 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 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..204
FT /note="Porphobilinogen deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01379"
FT DOMAIN 220..291
FT /note="Porphobilinogen deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03900"
SQ SEQUENCE 307 AA; 34078 MW; FC624F63C2BCF4B9 CRC64;
MAEKTIRIGT RDSELALWQA HTVEKKLNDL GYKTEIIAVK STGDIILDKP LYELGITGIF
TKTLDVAMIN GDVDIAVHSM KDVPTALPKG IVQAAVLERA NVLDILVHKG NPDFANPSTI
ATGSLRRQAQ WFNKYPNHTV VDLRGNVNTR MQKLQDNNWD GAVFAAAGLE RINLKPENYI
DLDWMIPAPA QGAMVVVAME NDNYALEALS QLNDIETEIC TYIERQFLRT LEGGCTAPIG
ALVRYNEEED TLHFQGVLLS VDGKQKLEIN KTVEIGEWKK LGFFAAQEIL NNGGTELMQA
IKESLKK
//
