ID B7GQV2_BIFLS Unreviewed; 491 AA. AC B7GQV2; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 24-JAN-2024, entry version 77. DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106}; DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106}; GN OrderedLocusNames=Blon_1092 {ECO:0000313|EMBL:ACJ52182.1}; OS Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM OS 1222 / NCTC 11817 / S12). OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=391904 {ECO:0000313|EMBL:ACJ52182.1, ECO:0000313|Proteomes:UP000001360}; RN [1] {ECO:0000313|EMBL:ACJ52182.1, ECO:0000313|Proteomes:UP000001360} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12 [JGI] RC {ECO:0000313|Proteomes:UP000001360}; RX PubMed=19033196; DOI=10.1073/pnas.0809584105; RA Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R., RA Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P., RA Richardson P.M., Mills D.A.; RT "The genome sequence of Bifidobacterium longum subsp. infantis reveals RT adaptations for milk utilization within the infant microbiome."; RL Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933}; CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}. 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; CP001095; ACJ52182.1; -; Genomic_DNA. DR AlphaFoldDB; B7GQV2; -. DR SMR; B7GQV2; -. DR KEGG; bln:Blon_1092; -. DR Proteomes; UP000001360; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. 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 CDD; cd00093; HTH_XRE; 1. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 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; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR PANTHER; PTHR43488; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1. DR PANTHER; PTHR43488:SF2; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 3: Inferred from homology; KW Aminotransferase {ECO:0000313|EMBL:ACJ52182.1}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125}; KW Transferase {ECO:0000313|EMBL:ACJ52182.1}. FT DOMAIN 24..56 FT /note="HTH cro/C1-type" FT /evidence="ECO:0000259|PROSITE:PS50943" FT REGION 58..89 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 491 AA; 54714 MW; BB05A74186F81D19 CRC64; MNSRGLKQVD LVHAAEHRGV KMGKSHISQY VAGKTMPRED VLEFLASELD VDANWLRGEE SSAPSNGDAA PEGAGPRTDD GTAPARRRTF GKSHKLDNVL YDVRGPVADE AMRMEANGTH ILKLNIGNPA PFGFRTPDEV VYDMAHQLTD TEGYSPSKGL FSARKAIMQY AQLKNIPNVT IDDIYTGNGV SELINLSMSA LLDTGDEVLV PSPDYPLWTA CVNLAGGTAV HYLCDEQSEW YPDIDDIRSK ITSNTKAIVI INPNNPTGAL YPKEVLQQIV DIARERRLII FSDEIYDRLV MDGLQHVSIA SMAPDLFCVT FSGLSKSHMI AGYRIGWMIL SGNKRIAKDY IEGLNMLANM RMCSNVPAQS VVQTALGGHQ SVKDYLVPGG RVYDQRDLVY DMLNAIPGIS AVKPKAAFYI FPKIDVKRFN IHSDEQFALD LLHEKHILIS HGGAFNWRHP DHFRVVYLPR IGMLHETMEE LADFFSYYRQ N //