ID Q97I35_CLOAB Unreviewed; 398 AA.
AC Q97I35;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN Name=aspB {ECO:0000313|EMBL:AAK79784.1};
GN OrderedLocusNames=CA_C1819 {ECO:0000313|EMBL:AAK79784.1};
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK79784.1, ECO:0000313|Proteomes:UP000000814};
RN [1] {ECO:0000313|EMBL:AAK79784.1, ECO:0000313|Proteomes:UP000000814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC {ECO:0000313|Proteomes:UP000000814};
RX PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC ECO:0000256|RuleBase:RU000481}.
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DR EMBL; AE001437; AAK79784.1; -; Genomic_DNA.
DR PIR; E97124; E97124.
DR RefSeq; NP_348444.1; NC_003030.1.
DR RefSeq; WP_010965125.1; NC_003030.1.
DR AlphaFoldDB; Q97I35; -.
DR STRING; 272562.CA_C1819; -.
DR KEGG; cac:CA_C1819; -.
DR PATRIC; fig|272562.8.peg.2025; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_9; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00753; ACCSYNTHASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:AAK79784.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000814};
KW Transferase {ECO:0000256|RuleBase:RU000481}.
FT DOMAIN 31..385
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 398 AA; 43976 MW; 689E2161DD05107C CRC64;
MNFSKKAGQI AASITLEITA KADEMKANGI NVIGFGAGQP DFNTPKNIRD AAIYAIENGY
TKYTPVSGIK ELKMAICDKF KRDNNLNYSL SNIIVSTGAK QCLSDTFSAL LNPGDEVILS
APYWVTYPEL IKLNDGISVI INTTEENHFK LSVDDLENAY TSKTKAILIN SPSNPTGTVY
TETELKAIAE FAKEKDLFII SDEIYEKLIY DGERHVSIAS LSQDAFNRTV VINGMSKSYA
MTGWRLGYAA SGSSEFIKLM SHIQAHTTSN ANSITQYASV EALNGRQEEL HSMVTEFEKR
RTYMSKRVNN ITGIHCLLPK GAFYVMMNIS NLFGKEINGV KINNSVDFSK ELLSENKVAV
VPGTGFGNDN YVRLSYATSM DNIVKGLDEI ENFIGKLR
//
