1A1D_RHILV
ID 1A1D_RHILV Reviewed; 339 AA.
AC Q93AG0;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=1-aminocyclopropane-1-carboxylate deaminase {ECO:0000255|HAMAP-Rule:MF_00807};
DE Short=ACC deaminase {ECO:0000255|HAMAP-Rule:MF_00807};
DE Short=ACCD {ECO:0000255|HAMAP-Rule:MF_00807};
DE EC=3.5.99.7 {ECO:0000255|HAMAP-Rule:MF_00807};
GN Name=acdS {ECO:0000255|HAMAP-Rule:MF_00807};
OS Rhizobium leguminosarum bv. viciae.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=387;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=128c53;
RX PubMed=12902221; DOI=10.1128/aem.69.8.4396-4402.2003;
RA Ma W., Guinel F.C., Glick B.R.;
RT "Rhizobium leguminosarum biovar viciae 1-aminocyclopropane-1-carboxylate
RT deaminase promotes nodulation of pea plants.";
RL Appl. Environ. Microbiol. 69:4396-4402(2003).
CC -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the
CC irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to
CC ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen
CC source.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00807};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00807};
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00807}.
CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC family. {ECO:0000255|HAMAP-Rule:MF_00807}.
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DR EMBL; AF421376; AAL16088.1; -; Genomic_DNA.
DR RefSeq; WP_018481130.1; NZ_WIEO01000091.1.
DR AlphaFoldDB; Q93AG0; -.
DR SMR; Q93AG0; -.
DR GeneID; 66143936; -.
DR BRENDA; 3.5.99.7; 5343.
DR GO; GO:0008660; F:1-aminocyclopropane-1-carboxylate deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0018871; P:1-aminocyclopropane-1-carboxylate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009310; P:amine catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1100; -; 2.
DR HAMAP; MF_00807; ACC_deaminase; 1.
DR InterPro; IPR027278; ACCD_DCysDesulf.
DR InterPro; IPR005965; ACP_carboxylate_deaminase.
DR InterPro; IPR020601; ACP_carboxylate_deaminase_bac.
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; TIGR01274; ACC_deam; 1.
PE 3: Inferred from homology;
KW Hydrolase; Pyridoxal phosphate.
FT CHAIN 1..339
FT /note="1-aminocyclopropane-1-carboxylate deaminase"
FT /id="PRO_0000184507"
FT ACT_SITE 79
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00807"
FT MOD_RES 52
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00807"
SQ SEQUENCE 339 AA; 36607 MW; B736AB026D982A6B CRC64;
MSLLEKFERY PLTFGPTPIE HLPRLTAALG GKVDIYAKRD DCNSGLAMGG NKLRKLEYIV
PDAIASGADT LVSIGGVQSN HTRMVAATAA KIGMKCVVIQ EKWVPHYDAV YDRVGNILMT
KLMGADSRLV EDGFDIGIRK SWEDAIQSVE DAGGKPYAIP AGASVHKFGG LGYVGFAEEV
AAQEKDLGFI FDYIIVCVVT GSTQGGMIVG FAALDRADRV IGIDASGTLQ QTRDQVRKIV
DATSELVNLG RSVREDEIVI NPDYAYPAYG VPSEETNEAI RLAARTEAMI TDPVYEGKSM
QGMIDLARKG FFPEGSKVLY AHLGGAPALN GYSYYYKDG
