ID D5V4U0_ARCNC Unreviewed; 370 AA.
AC D5V4U0;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Aminotransferase class V {ECO:0000313|EMBL:ADG91902.1};
GN OrderedLocusNames=Arnit_0236 {ECO:0000313|EMBL:ADG91902.1};
OS Arcobacter nitrofigilis (strain ATCC 33309 / DSM 7299 / CCUG 15893 / LMG
OS 7604 / NCTC 12251 / CI) (Campylobacter nitrofigilis).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Arcobacteraceae; Arcobacter.
OX NCBI_TaxID=572480 {ECO:0000313|EMBL:ADG91902.1, ECO:0000313|Proteomes:UP000000939};
RN [1] {ECO:0000313|EMBL:ADG91902.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7299 {ECO:0000313|EMBL:ADG91902.1};
RX PubMed=21304714; DOI=10.4056/sigs.912121;
RA Pati A., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T., Nolan M.,
RA Lucas S., Tice H., Cheng J.F., Han C., Chertkov O., Bruce D., Tapia R.,
RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Arcobacter nitrofigilis type strain (CI).";
RL Stand. Genomic Sci. 2:300-308(2010).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50, ECO:0000256|RuleBase:RU004504};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU004075}.
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DR EMBL; CP001999; ADG91902.1; -; Genomic_DNA.
DR RefSeq; WP_013134047.1; NC_014166.1.
DR AlphaFoldDB; D5V4U0; -.
DR STRING; 572480.Arnit_0236; -.
DR KEGG; ant:Arnit_0236; -.
DR eggNOG; COG0075; Bacteria.
DR HOGENOM; CLU_027686_1_1_7; -.
DR OrthoDB; 9766472at2; -.
DR Proteomes; UP000000939; Chromosome.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR PANTHER; PTHR42778; 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE; 1.
DR PANTHER; PTHR42778:SF1; 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ADG91902.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000000939};
KW Transferase {ECO:0000313|EMBL:ADG91902.1}.
FT DOMAIN 22..312
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 183
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 370 AA; 40682 MW; 526A6DF8AB102DAD CRC64;
MLLTPGPTPV PEFVRKAMAD ITIHHRTPEF ESIFGQTREL LLELYGMDEV VMLASSGTGA
MEACILNLVN KKALTINSGK FGERFGKICK AYNLPYTEIK NEWNTPVSVE EVMDTLKNDS
EIDAIFIQIC ESAGGLRHPV EELAKQVKEF NKNIMIVADG ITAVGVEKID TTNLDAVITG
SQKALMLPPG LAMIGLSNVA VEKIQTLSKG YYFNLATEIK VQKTNTTAWT AATTLIIGLK
EILTHIKNNG GFETLYEKTA LRAKATREAL KAIGCEIYPK MPANAMTTIY TENAPAIRKI
LKTKYNVNIA GGQDHIKNSI FRINHMGLVE DFETAWAVNA VELAMDELGL RAFDGTANKI
FAMVTFKGNE
//
