ID Q7VBS4_PROMA Unreviewed; 393 AA.
AC Q7VBS4;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN OrderedLocusNames=Pro_1018 {ECO:0000313|EMBL:AAQ00063.1};
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=167539 {ECO:0000313|EMBL:AAQ00063.1, ECO:0000313|Proteomes:UP000001420};
RN [1] {ECO:0000313|EMBL:AAQ00063.1, ECO:0000313|Proteomes:UP000001420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120 {ECO:0000313|Proteomes:UP000001420};
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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; AE017126; AAQ00063.1; -; Genomic_DNA.
DR RefSeq; NP_875410.1; NC_005042.1.
DR RefSeq; WP_011125170.1; NC_005042.1.
DR AlphaFoldDB; Q7VBS4; -.
DR STRING; 167539.Pro_1018; -.
DR EnsemblBacteria; AAQ00063; AAQ00063; Pro_1018.
DR KEGG; pma:Pro_1018; -.
DR PATRIC; fig|167539.5.peg.1069; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_3; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000001420; 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:AAQ00063.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001420};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:AAQ00063.1}.
FT DOMAIN 35..385
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 393 AA; 42983 MW; 5849D52ABB5FAB81 CRC64;
MSNLDVISER ALSLKPSLTL EISSLAQSLK QKGRDICSLS AGEPDFDTPN FIVEAAKKAL
DDGITKYGPA GGDPSLREEV AKKLTEINDV PTSPENVLIT NGGKQAIFNL LQVIINPGDE
VLIPSPYWLS YPEITKIAGG IPITINSSKG NSFSLDIEEI EKNINHKTKL LILNSPCNPT
GRIIQESELQ SIANLLRKHP NIYVMSDEIY EFLITDKEVH ISLASIAPDL KDKIFIVNGF
AKAWAMTGWR VGYLQGSSKI IKKAIALQSQ STSNVCSFAQ RGALAAIKGA PKGIDYMIQS
YNERRKLLTE ELRQISSLSL EAQSGAFYAF PKLSDELPDS LSFCKIALEK EGLAIVPGIA
FGNDRCIRLS CSVNTETLND GITRLNRIIK DIT
//
