1A1D_PYRAB
ID 1A1D_PYRAB Reviewed; 330 AA.
AC Q9V2L2; G8ZFP4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Putative 1-aminocyclopropane-1-carboxylate deaminase;
DE Short=ACC deaminase;
DE EC=3.5.99.7;
GN OrderedLocusNames=PYRAB00630; ORFNames=PAB2303;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate +
CC NH4(+); Xref=Rhea:RHEA:16933, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:58360; EC=3.5.99.7;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC family. {ECO:0000305}.
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DR EMBL; AJ248283; CAB48986.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69435.1; -; Genomic_DNA.
DR PIR; C75192; C75192.
DR RefSeq; WP_010867187.1; NC_000868.1.
DR AlphaFoldDB; Q9V2L2; -.
DR SMR; Q9V2L2; -.
DR STRING; 272844.PAB2303; -.
DR EnsemblBacteria; CAB48986; CAB48986; PAB2303.
DR GeneID; 1494946; -.
DR KEGG; pab:PAB2303; -.
DR PATRIC; fig|272844.11.peg.70; -.
DR eggNOG; arCOG01435; Archaea.
DR HOGENOM; CLU_048897_1_0_2; -.
DR OMA; LVQEKWV; -.
DR OrthoDB; 35277at2157; -.
DR PhylomeDB; Q9V2L2; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
DR GO; GO:0008660; F:1-aminocyclopropane-1-carboxylate deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR027278; ACCD_DCysDesulf.
DR InterPro; IPR005966; D-Cys_desShydrase.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR PANTHER; PTHR43780; PTHR43780; 1.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF006278; ACCD_DCysDesulf; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR01275; ACC_deam_rel; 1.
PE 3: Inferred from homology;
KW Hydrolase; Pyridoxal phosphate.
FT CHAIN 1..330
FT /note="Putative 1-aminocyclopropane-1-carboxylate
FT deaminase"
FT /id="PRO_0000184521"
FT MOD_RES 54
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 330 AA; 35755 MW; CC8699923C0B11CD CRC64;
MHPKVDALLS RFPRITLIPW ETPIQYLPRI SRELGVDVYV KRDDLTGLGI GGNKIRKLEF
LLGDALSRGC DTVITIGAVH SNHAFVTALA AKKLGLGAVL ILRGEEVLKG NYLLDKLMGI
ETRIYEADNS WELMKVAEEV AEELKGEGKK PYIIPPGGAS PVGTLGYIRG VGELYTQVKK
LGLRIDTVVD AVGSGGTYAG LLLGSAIVNA EWSVVGIDVS SATEKAKERV KNLVEKTKEL
LGINVKVQEP RIYDYGFGAY GKIVKEVAKL IKSVGTMEGL LLDPVYTGKA FYGLMDLAKK
GDLGESVLFI HTGGLPGIFH YGEEMLELLV
