ID A0A2A9EEP7_9MICO Unreviewed; 335 AA.
AC A0A2A9EEP7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=hydroxymethylbilane synthase {ECO:0000256|ARBA:ARBA00012655};
DE EC=2.5.1.61 {ECO:0000256|ARBA:ARBA00012655};
GN ORFNames=ATL41_1765 {ECO:0000313|EMBL:PFG37021.1};
OS Flavimobilis soli.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Jonesiaceae;
OC Flavimobilis.
OX NCBI_TaxID=442709 {ECO:0000313|EMBL:PFG37021.1, ECO:0000313|Proteomes:UP000221394};
RN [1] {ECO:0000313|EMBL:PFG37021.1, ECO:0000313|Proteomes:UP000221394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21574 {ECO:0000313|EMBL:PFG37021.1,
RC ECO:0000313|Proteomes:UP000221394};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2017) 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:PFG37021.1}.
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DR EMBL; PDJH01000001; PFG37021.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9EEP7; -.
DR OrthoDB; 9810298at2; -.
DR Proteomes; UP000221394; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000221394};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..213
FT /note="Porphobilinogen deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01379"
FT DOMAIN 229..275
FT /note="Porphobilinogen deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03900"
SQ SEQUENCE 335 AA; 33936 MW; 47379808ED363ECF CRC64;
MTATTVRIGT RASALARTQT GHVADALTSA AAAAGVDVRV KTVPVTTEGD RSRASLAQLG
GTGVFVTALR DALLADVCDL AVHSLKDLPT APAPGLEIVA TPERVSPLDA LCARDGLDLA
GLPRGARVGT GSPRRKAQLL AARPDLEVVD IRGNVETRLA RALGADADLH AVVLAAAGLA
RLGRSDVVSE VLAPDVMMPA PGQGVLAVEQ RAGASFPGVA ALDHIPTRLA ATAERTLLAR
LEAGCAAPVG ALGTVSDDGR TLELQAVVAS LDGTRVLRHG ASSVCSAAWL PGEPRPTDEE
LTASLVHDVQ SAATLGADLA DLLLDLGAAD IAPLR
//
