ID C5AIK3_BURGB Unreviewed; 361 AA.
AC C5AIK3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 OrderedLocusNames=bglu_2g13730 {ECO:0000313|EMBL:ACR31733.1};
OS Burkholderia glumae (strain BGR1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=626418 {ECO:0000313|EMBL:ACR31733.1, ECO:0000313|Proteomes:UP000002187};
RN [1] {ECO:0000313|EMBL:ACR31733.1, ECO:0000313|Proteomes:UP000002187}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGR1 {ECO:0000313|EMBL:ACR31733.1,
RC ECO:0000313|Proteomes:UP000002187};
RX PubMed=19329631; DOI=10.1128/JB.00349-09;
RA Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.;
RT "Complete genome sequence of Burkholderia glumae BGR1.";
RL J. Bacteriol. 191:3758-3759(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; CP001504; ACR31733.1; -; Genomic_DNA.
DR AlphaFoldDB; C5AIK3; -.
DR STRING; 626418.bglu_2g13730; -.
DR KEGG; bgl:bglu_2g13730; -.
DR eggNOG; COG2515; Bacteria.
DR HOGENOM; CLU_048897_2_1_4; -.
DR Proteomes; UP000002187; Chromosome 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000002187}.
FT DOMAIN 35..344
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT ACT_SITE 101
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00807,
FT ECO:0000256|PIRSR:PIRSR006278-1"
FT MOD_RES 74
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00807,
FT ECO:0000256|PIRSR:PIRSR006278-2"
SQ SEQUENCE 361 AA; 38725 MW; EA7C4E6C2F9D8A43 CRC64;
MGAGSGATGV VRNVSIHPFK ERDMNLQKFP RYPLTFGPTP IQPLRRLSAH LGGKVELYAK
REDCNSGLAF GGNKTRKLEY LIPDAIAQGA DTLVSIGGVQ SNQTRQVAAV AAHLGMKCVL
VQENWVNYSD AVYDRVGNIQ MSRMMGADVR LVPDGFDIGI RKSWEDALAE VRAAGGKPYP
IPAGCSEHPL GGLGFVAFAE EVRAQEVELG IRFDYIVVCS VTGSTQAGMV VGFAADGRAD
RVIGIDASAK PAQTREQILR IARGTADRVE LGRDIGEADV VLDERFGGPE YGLPSDGTLE
AIRLSARLEG MLTDPVYEGK SMHGMIEKVR LGEFPAGAKV LYAHLGGVPA LSAYSYLFRD
G
//
