ID F4XIA1_9CYAN Unreviewed; 408 AA.
AC F4XIA1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=LYNGBM3L_01610 {ECO:0000313|EMBL:EGJ35634.1};
OS Moorena producens 3L.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Moorena.
OX NCBI_TaxID=489825 {ECO:0000313|EMBL:EGJ35634.1, ECO:0000313|Proteomes:UP000003959};
RN [1] {ECO:0000313|Proteomes:UP000003959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3L {ECO:0000313|Proteomes:UP000003959};
RX PubMed=21555588; DOI=10.1073/pnas.1101137108;
RA Jones A.C., Monroe E.A., Podell S., Hess W.R., Klages S., Esquenazi E.,
RA Niessen S., Hoover H., Rothmann M., Lasken R.S., Yates J.R.III.,
RA Reinhardt R., Kube M., Burkart M.D., Allen E.E., Dorrestein P.C.,
RA Gerwick W.H., Gerwick L.;
RT "Genomic insights into the physiology and ecology of the marine filamentous
RT cyanobacterium Lyngbya majuscula.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:8815-8820(2011).
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|RuleBase:RU000481}.
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DR EMBL; GL890816; EGJ35634.1; -; Genomic_DNA.
DR RefSeq; WP_008177694.1; NZ_MKZR01000001.1.
DR AlphaFoldDB; F4XIA1; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_5_3; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000003959; Unassembled WGS sequence.
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; PTHR42832; AMINO ACID AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42832:SF2; ASPARTATE TRANSAMINASE; 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:EGJ35634.1};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:EGJ35634.1}.
FT DOMAIN 30..400
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 408 AA; 44117 MW; 56A9972DFE00486F CRC64;
MQFAQRLQPL QANVFADMDQ AKALAAAGKE IIDLSLGSSD LPAPKHVCAA IEASLYDPST
HGYLLFHGTK AFRQAAASWY TKKFGIPVDP ETEVLQLIGS QEGTAHLPLA VLNPGDFALL
QDPGYPSHAG GVHLASGQIY PMPLLAENNF LPVFEDIPQA VLAQARMMVL SYPHNPTTAI
APLSFFQEAV AFCQCHNLVL VHDFPYVDIV FEDTTGNGEQ IGKIPESLNP TSVAPSVLQA
DPDKTVSIEF FSFSKSYNMG GFRIGYAIGN AQVIRALRQV KAAIDFNQYR GILNGAIAAL
NGSQDIVKPV VTTYQQRRDT FVDALNRIGW SVPVPLATMY VWAKLPEPWA GNSVKFCTSL
VEATGVAVAP GAGFGKAGEG YVRFALVQEP EVLERAVERI SGFLQSHQ
//
