ID B7K947_GLOC7 Unreviewed; 441 AA. AC B7K947; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAR-2024, entry version 86. DE SubName: Full=Acetylornithine transaminase {ECO:0000313|EMBL:ACK72816.1}; DE EC=2.6.1.11 {ECO:0000313|EMBL:ACK72816.1}; GN OrderedLocusNames=PCC7424_4452 {ECO:0000313|EMBL:ACK72816.1}; OS Gloeothece citriformis (strain PCC 7424) (Cyanothece sp. (strain PCC OS 7424)). OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae; OC Chroococcales; Aphanothecaceae; Gloeothece; Gloeothece citriformis. OX NCBI_TaxID=65393 {ECO:0000313|EMBL:ACK72816.1, ECO:0000313|Proteomes:UP000002384}; RN [1] {ECO:0000313|Proteomes:UP000002384} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7424 {ECO:0000313|Proteomes:UP000002384}; RX PubMed=21972240; DOI=10.1128/mBio.00214-11; RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H., RA Sherman L.A., Pakrasi H.B.; RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of RT unicellular nitrogen-fixing Cyanobacteria."; RL MBio 2:E214-E214(2011). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001291; ACK72816.1; -; Genomic_DNA. DR RefSeq; WP_015956400.1; NC_011729.1. DR AlphaFoldDB; B7K947; -. DR STRING; 65393.PCC7424_4452; -. DR KEGG; cyc:PCC7424_4452; -. DR eggNOG; COG0160; Bacteria. DR HOGENOM; CLU_016922_10_0_3; -. DR OrthoDB; 9807885at2; -. DR Proteomes; UP000002384; Chromosome. DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase 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:ACK72816.1}; 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:UP000002384}; KW Transferase {ECO:0000313|EMBL:ACK72816.1}. SQ SEQUENCE 441 AA; 47741 MW; CD422F6B80D664EA CRC64; MLNISTSQTL PQVPKLITPL PGKRASELIN RDNAVTSPSY TRDYPLVVAR GQGCMIEDVD GNVFLDMTAG IAVTATGHCH PQVVEAIQYQ STQLVHMSGT DFYYAPMVDL AEKLAEKAPF PTPVTGSRAK VFFTNSGAES TECAIKLARY YTGRSRLIAF LGAFHGRTYG AMSLTGSKRV QRQGFGPLVP GVTHIPYGTH AGLDDLEEKL FTSIVPPDEV AAIMVEPIQG EGGYLVPEDG FLERIRSICD RYGILMIVDE VQAGMGRTGK LFAIEHWGIM PDMITLAKGI ASGLPLGAVL SRPELMTWPP GSHATTFGGN PIACAAGKVT LDLLEGGLME NATQRGEELL LGLTQLSQRF DRLSLPRGKG LMIGIDLLDR EGNLDPVLRN YVLNEAFYRG LLLLGCGKAA IRFCPPLVIS GEQIEVALKI LAEILEEVVR R //