ID E1VRN7_GLUAR Unreviewed; 262 AA.
AC E1VRN7;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Enoyl-CoA hydratase/isomerase family protein {ECO:0000313|EMBL:CBT74290.1};
GN OrderedLocusNames=AARI_00480 {ECO:0000313|EMBL:CBT74290.1};
OS Glutamicibacter arilaitensis (strain DSM 16368 / CIP 108037 / IAM 15318 /
OS JCM 13566 / NCIMB 14258 / Re117) (Arthrobacter arilaitensis).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Glutamicibacter.
OX NCBI_TaxID=861360 {ECO:0000313|Proteomes:UP000006878};
RN [1] {ECO:0000313|EMBL:CBT74290.1, ECO:0000313|Proteomes:UP000006878}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC {ECO:0000313|Proteomes:UP000006878};
RX PubMed=21124797; DOI=10.1371/journal.pone.0015489;
RA Monnet C., Loux V., Gibrat J.F., Spinnler E., Barbe V., Vacherie B.,
RA Gavory F., Gourbeyre E., Siguier P., Chandler M., Elleuch R., Irlinger F.,
RA Vallaeys T.;
RT "The Arthrobacter arilaitensis Re117 genome sequence reveals its genetic
RT adaptation to the surface of cheese.";
RL PLoS ONE 5:E15489-E15489(2010).
RN [2] {ECO:0000313|Proteomes:UP000006878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC {ECO:0000313|Proteomes:UP000006878};
RA Genoscope.;
RT "Complete genome sequence of Arthrobacter arilaitensis (strain DSM 16368 /
RT CIP 108037 / JCM 13566 / Re117).";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000256|ARBA:ARBA00005254, ECO:0000256|RuleBase:RU003707}.
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DR EMBL; FQ311875; CBT74290.1; -; Genomic_DNA.
DR RefSeq; WP_013347444.1; NC_014550.1.
DR AlphaFoldDB; E1VRN7; -.
DR STRING; 861360.AARI_00480; -.
DR KEGG; aai:AARI_00480; -.
DR eggNOG; COG1024; Bacteria.
DR HOGENOM; CLU_009834_7_6_11; -.
DR OrthoDB; 9790967at2; -.
DR Proteomes; UP000006878; Chromosome.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProt.
DR CDD; cd06558; crotonase-like; 1.
DR Gene3D; 1.10.12.10; Lyase 2-enoyl-coa Hydratase, Chain A, domain 2; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR PANTHER; PTHR11941:SF54; ENOYL-COA HYDRATASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11941; ENOYL-COA HYDRATASE-RELATED; 1.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:CBT74290.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006878}.
SQ SEQUENCE 262 AA; 27779 MW; 1F0F47C205268975 CRC64;
MKQFDTLSLS TQGSALIVTV NQPKSLNALA KEVVNDLEAF LDWFQGTGFA YRGVILTGAG
EKSFVAGANI VQLREMDPEA ALAYGRQMHA VTERLEKLQV PVIAAVNGFA LGGGCELALA
CDFIYASESA SFGQPEVNLG LVPGFGGMVR LPRRVGNAMA RELIFTGRRI KAAEALRIGL
ANRVVPAGEL IDQAVAAIEE VAKVAPTAVA NAKNALMDMD GLNTHDALLV EADSFQQAFK
TADSVEGRAA FVEKRAPQFP GN
//
