ID A9BA56_PROM4 Unreviewed; 393 AA.
AC A9BA56;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN Name=aspC {ECO:0000313|EMBL:ABX08718.1};
GN OrderedLocusNames=P9211_07871 {ECO:0000313|EMBL:ABX08718.1};
OS Prochlorococcus marinus (strain MIT 9211).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=93059 {ECO:0000313|EMBL:ABX08718.1, ECO:0000313|Proteomes:UP000000788};
RN [1] {ECO:0000313|EMBL:ABX08718.1, ECO:0000313|Proteomes:UP000000788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9211 {ECO:0000313|Proteomes:UP000000788};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000878; ABX08718.1; -; Genomic_DNA.
DR RefSeq; WP_012195340.1; NC_009976.1.
DR AlphaFoldDB; A9BA56; -.
DR STRING; 93059.P9211_07871; -.
DR KEGG; pmj:P9211_07871; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_3; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000000788; 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 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:ABX08718.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000788};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ABX08718.1}.
FT DOMAIN 35..385
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 393 AA; 43112 MW; 04E65DC5C81303AA CRC64;
MSKSHLISER TQELQLSLTL EISARAKLLK KEGKDICSLS AGEPDFDTPN YIVNAAIEAL
RNGITRYGPA AGDPELREAI AQKLTTSNNV PSKAENILIT NGGKQAIFNL FQIILNPGDE
VLIPSPYWLS YPEIAKLAGA IPVPLHTSPK DGFKLSSEKL EEKITNRTKL LILNSPCNPT
GRVIQKEELI SIAEVLRRNK QLLVMTDEIY EYLISENESH HSLAAIAPDL RERIFIVNGF
AKAWAMTGWR IGYLAGPKEF IKTAIALQSQ STSNVCSFAQ RGALAALLGP KESIKTMSRS
YNERREILTK GLNSINGISL IPQKGAFYAF PELAPSLPNS LSFCKLALEK VGLAIIPGIA
FGEDRCVRLS CAVSEDTIKE GIARLEKLIT QLI
//
