ID A0A0C1RII8_9CYAN Unreviewed; 452 AA.
AC A0A0C1RII8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:KIE11795.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:KIE11795.1};
DE SubName: Full=Acetyl ornithine aminotransferase family protein {ECO:0000313|EMBL:KAF3884756.1};
GN ORFNames=DA73_0213255 {ECO:0000313|EMBL:KIE11795.1}, DA73_0400004250
GN {ECO:0000313|EMBL:KAF3884756.1};
OS Tolypothrix bouteillei VB521301.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE11795.1};
RN [1] {ECO:0000313|EMBL:KIE11795.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KIE11795.1};
RX PubMed=25700407;
RA Chandrababunaidu M.M., Singh D., Sen D., Bhan S., Das S., Gupta A.,
RA Adhikary S.P., Tripathy S.;
RT "Draft Genome Sequence of Tolypothrix boutellei Strain VB521301.";
RL Genome Announc. 3:e00001-15(2015).
RN [2] {ECO:0000313|EMBL:KAF3884756.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KAF3884756.1};
RA Sarangi A.N., Mukherjee M., Ghosh S., Singh D., Das A., Kant S., Prusty A.,
RA Tripathy S.;
RT "Improved Assembly of Tolypothrix boutellei genome.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIE11795.1}.
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DR EMBL; JHEG04000001; KAF3884756.1; -; Genomic_DNA.
DR EMBL; JHEG02000040; KIE11795.1; -; Genomic_DNA.
DR RefSeq; WP_038083722.1; NZ_JHEG04000001.1.
DR AlphaFoldDB; A0A0C1RII8; -.
DR STRING; 1479485.DA73_0213255; -.
DR OrthoDB; 9807885at2; -.
DR Proteomes; UP000029738; Unassembled WGS sequence.
DR GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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; 2.
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:KIE11795.1};
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:UP000029738};
KW Transferase {ECO:0000313|EMBL:KIE11795.1}.
SQ SEQUENCE 452 AA; 48687 MW; 16DC271FB58E904E CRC64;
MLELSQSKIE NRKSKISLPC KPHIITSLPG SKTLDLVERD RAVTSPSYTR DYPLVVARGE
GCMVEDVDGN VFLDMTAGIA VTATGHCHPE VVRAIQEQAA NLIHMSGTDF YYEPMVELAE
KLASRAPFPP VVGEGTGKTS FPAKVFFTNS GAESNEGAIK LARYYTGRSL IIAFLGAFHG
RTYGAMSLTG SKTVQRANFG PLVPGVTHIP YGTHASLDYL EKQLFPTMLP PKEVAAIVVE
AIQGEGGYIV PEDGFLQRIR EICDRHGMLM VVDEVQAGMG RTGRLFAIEH WGVMPDIITT
AKGIASGLPL GAILSRPEIM TWSPGSHATT FGGNPVACAA AIATLKLLES GLMANATAMG
EVLQAGLHRL SQQFPQVSSP RGKGLMVAVD LLDCEGNYNS QLRDRIVQRA FLKGLLLLGC
GKAAIRFCPP LIIDRNQIEI ALDILAEVLI EM
//
