ID B8R7T3_9BURK Unreviewed; 338 AA.
AC B8R7T3;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=1-aminocyclopropane-1-carboxylate deaminase {ECO:0000256|HAMAP-Rule:MF_00807};
DE Short=ACC deaminase {ECO:0000256|HAMAP-Rule:MF_00807};
DE Short=ACCD {ECO:0000256|HAMAP-Rule:MF_00807};
DE EC=3.5.99.7 {ECO:0000256|HAMAP-Rule:MF_00807};
GN Name=acdS {ECO:0000256|HAMAP-Rule:MF_00807,
GN ECO:0000313|EMBL:ACH81535.1};
OS Paraburkholderia xenovorans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=36873 {ECO:0000313|EMBL:ACH81535.1};
RN [1] {ECO:0000313|EMBL:ACH81535.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCUG 28445 {ECO:0000313|EMBL:ACH81535.1};
RX PubMed=19700546; DOI=10.1128/AEM.01240-09;
RA Onofre-Lemus J., Hernandez-Lucas I., Girard L., Caballero-Mellado J.;
RT "ACC (1-aminocyclopropane-1-carboxylate) deaminase activity, a widespread
RT trait in Burkholderia species, and its growth-promoting effect on tomato
RT plants.";
RL Appl. Environ. Microbiol. 75:6581-6590(2009).
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. {ECO:0000256|ARBA:ARBA00003003, ECO:0000256|HAMAP-
CC Rule:MF_00807}.
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:0000256|ARBA:ARBA00001132, ECO:0000256|HAMAP-
CC Rule:MF_00807};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00807};
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00807}.
CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC family. {ECO:0000256|ARBA:ARBA00008639, ECO:0000256|HAMAP-
CC Rule:MF_00807}.
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DR EMBL; EU886313; ACH81535.1; -; Genomic_DNA.
DR AlphaFoldDB; B8R7T3; -.
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 CDD; cd06449; ACCD; 1.
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; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01274; ACC_deam; 1.
DR PANTHER; PTHR43780; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE-RELATED; 1.
DR PANTHER; PTHR43780:SF2; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF006278; ACCD_DCysDesulf; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00807};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00807}.
FT DOMAIN 12..321
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT ACT_SITE 78
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00807,
FT ECO:0000256|PIRSR:PIRSR006278-1"
FT MOD_RES 51
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00807,
FT ECO:0000256|PIRSR:PIRSR006278-2"
SQ SEQUENCE 338 AA; 36682 MW; 230B55E9EE4C5FBA CRC64;
MNLQRFPRYP LTFGPTPIQP LARLSKHLGG KVHLYAKRED CNSGLAFGGN KTRKLEYLIP
EVLAQGCDTL VSIGGIQSNQ TRQVAAVAAH LGMKCVLVQE NWVNYSDAVY DRVGNIQMSR
ILGADVRLVP DGFDIGFRKS WEEALESVRA AGGKPYAIPA GCSDHPLGGL GFVGFAEEVR
RQEAELGFKF DYVVVCSVTG SKQAGMVVGF AADGRADRVI GIDASAKPAQ TREQITRIAR
QTAEKVGLGR DITSEDVVLD ERFAGPEYGL PNDGTLEAIR LCARMEGVLT DPVYEGKSMH
GMIEMVRNGE FPEGSRVLYA HLGGVPALNG YSFIFRNG
//
