ID Q7NEN0_GLOVI Unreviewed; 439 AA.
AC Q7NEN0;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:BAC91790.1};
GN OrderedLocusNames=glr3849 {ECO:0000313|EMBL:BAC91790.1};
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221 {ECO:0000313|EMBL:BAC91790.1, ECO:0000313|Proteomes:UP000000557};
RN [1] {ECO:0000313|EMBL:BAC91790.1, ECO:0000313|Proteomes:UP000000557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421 {ECO:0000313|Proteomes:UP000000557};
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; BA000045; BAC91790.1; -; Genomic_DNA.
DR RefSeq; NP_926795.1; NC_005125.1.
DR RefSeq; WP_011143837.1; NC_005125.1.
DR AlphaFoldDB; Q7NEN0; -.
DR STRING; 251221.gene:10761366; -.
DR EnsemblBacteria; BAC91790; BAC91790; BAC91790.
DR KEGG; gvi:glr3849; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_3; -.
DR InParanoid; Q7NEN0; -.
DR OrthoDB; 9807885at2; -.
DR PhylomeDB; Q7NEN0; -.
DR Proteomes; UP000000557; Chromosome.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 3.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Aminotransferase {ECO:0000313|EMBL:BAC91790.1};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000000557};
KW Transferase {ECO:0000313|EMBL:BAC91790.1}.
SQ SEQUENCE 439 AA; 46990 MW; C5BB680D1D21ED14 CRC64;
MLSLPTKEAS LPRVPRLVGP LPGPRAQALI ARDEAVTSPS YTRGYPLVAA RGEGCMLEDV
DGNVFLDLTA GIAVTATGHA HPVVVRAIQE QAANLLHMSG TDFYYEPMAE LAEALCERAP
FPTAAGRPRA RVFFSNSGAE SNEGALKLAR YYTGRQQVVA FLGAFHGRTY GAMSLTGSRA
VQRQGFGPLV PGISHIPYGT HASLDYLEDK LFPAVLPPEE IAAIVVESIQ GEGGYIVPED
GFHERIRQIC TRHGILMVVD EVQAGMGRTG KLFAIEHWGV QPDIVTLAKG IASGLPLGAI
LSRPEIMTWP AGSHATTFGG NPVACAAANA TLKLLEAGLI ENAERMGRVL QAGLGQLADR
FSFVSASRGK GLMVAVDLFD AAGNLDRERR DQIVDLAFYR GLLLLGCGKA AIRFCPPLVI
DADQVRVALD ILRQIFEEQ
//
