ID A0A3S0AVF9_9ACTO Unreviewed; 589 AA.
AC A0A3S0AVF9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=hydroxymethylbilane synthase {ECO:0000256|ARBA:ARBA00012655};
DE EC=2.5.1.61 {ECO:0000256|ARBA:ARBA00012655};
GN ORFNames=EKN07_03940 {ECO:0000313|EMBL:RTE50357.1};
OS Actinobaculum sp. 352.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinobaculum.
OX NCBI_TaxID=2490946 {ECO:0000313|EMBL:RTE50357.1, ECO:0000313|Proteomes:UP000273303};
RN [1] {ECO:0000313|EMBL:RTE50357.1, ECO:0000313|Proteomes:UP000273303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=352 {ECO:0000313|EMBL:RTE50357.1,
RC ECO:0000313|Proteomes:UP000273303};
RA Zhu W.;
RL Submitted (NOV-2018) 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:RTE50357.1}.
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DR EMBL; RQSN01000002; RTE50357.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0AVF9; -.
DR OrthoDB; 9810298at2; -.
DR Proteomes; UP000273303; Unassembled WGS sequence.
DR GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004852; F:uroporphyrinogen-III synthase activity; IEA:InterPro.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06578; HemD; 1.
DR Gene3D; 3.40.50.10090; -; 2.
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; IPR036108; 4pyrrol_syn_uPrphyn_synt_sf.
DR InterPro; IPR003754; 4pyrrol_synth_uPrphyn_synth.
DR InterPro; IPR000860; HemC.
DR InterPro; IPR022419; Porphobilin_deaminase_cofac_BS.
DR InterPro; IPR022417; Porphobilin_deaminase_N.
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; PF02602; HEM4; 1.
DR Pfam; PF01379; Porphobil_deam; 1.
DR PRINTS; PR00151; PORPHBDMNASE.
DR SUPFAM; SSF69618; HemD-like; 1.
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:UP000273303};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RTE50357.1}.
FT DOMAIN 1..202
FT /note="Porphobilinogen deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01379"
FT DOMAIN 369..569
FT /note="Tetrapyrrole biosynthesis uroporphyrinogen III
FT synthase"
FT /evidence="ECO:0000259|Pfam:PF02602"
FT REGION 308..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 589 AA; 61844 MW; BCB32D3523195CC0 CRC64;
MRLGTRASAL AMTQSTLVAD RLRETGPDVE LVPVRTCGDR ERGSLKHLAG LGVFAAELRS
ALLRGDVDFA VHSLKDLPTE TVPGLVIAAI PQREVAADAM CARDGMRLID LPAGARVGTG
SPRRVAQLRA LRPDLVFVDI RGNIGTRLER VRPGDLDAVV LAAAGLRRLG LAGYITEELP
ILPAPGQGAL AVECRSDDEK TASILRTLDD PDSRLQAQEE REVLAVLGGG CAAPIAALGI
DGLLRAAVFA ADGSRHVAVT VPLHSGAGRI AAQCLLDDGA AAIADLGASR QSRLEEFHDD
VALWREGKAR EEGRPHSLRE GADTFPSREG AVAPPPGEEP GASSSHEEAW APFAWRKAEV
FLPREEGVLS AALRELGIVV TACPVQRRRL LTPNIPSDQL EQAQWSVITS ARTVGALKEL
GVQLPGRIAA VGHATARALE AAGYGVDLIP REESAAGLLA EFPRGGGHVF LPCSALAGPE
LADGLRGRGW QVDVQSVYTM EEVEISAAIR RRWQGGEFAV VVITSGSVAR TVDRVLGWPR
ATAVVALGPA TARVLDELGV AAEISPTPHA PDVAATVAQL VVKAGEAAL
//
