ID D4YPR8_9MICO Unreviewed; 406 AA.
AC D4YPR8;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN Name=aspB2 {ECO:0000313|EMBL:EFG46803.1};
GN ORFNames=HMPREF0183_1928 {ECO:0000313|EMBL:EFG46803.1};
OS Brevibacterium mcbrellneri ATCC 49030.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=585530 {ECO:0000313|EMBL:EFG46803.1, ECO:0000313|Proteomes:UP000005714};
RN [1] {ECO:0000313|EMBL:EFG46803.1, ECO:0000313|Proteomes:UP000005714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49030 {ECO:0000313|EMBL:EFG46803.1,
RC ECO:0000313|Proteomes:UP000005714};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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:EFG46803.1}.
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DR EMBL; ADNU01000053; EFG46803.1; -; Genomic_DNA.
DR RefSeq; WP_005885378.1; NZ_ADNU01000053.1.
DR AlphaFoldDB; D4YPR8; -.
DR STRING; 585530.HMPREF0183_1928; -.
DR eggNOG; COG0436; Bacteria.
DR OrthoDB; 9763453at2; -.
DR Proteomes; UP000005714; 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; 3.40.640.10; 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 PANTHER; PTHR46383:SF2; (5-FORMYLFURAN-3-YL)METHYL PHOSPHATE TRANSAMINASE; 1.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 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:EFG46803.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005714};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:EFG46803.1}.
FT DOMAIN 42..393
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 406 AA; 43685 MW; 99BBB455A2CCC4AD CRC64;
MNSSQPLPST LTRISDRAKV VRPFSVMNIL QRVAELEAQG RDIISLCVGE PLQGAPKAVR
TRAADIMTDG TSLGYSPAAG ILPLREALSG HYKRWYGLDI PAERFFVTTG SSGAFLLSFL
ACFDAGDRVA LARPGYAAYK NILAGQGIEV VELDCGPDER FQPTVELLDQ AHSEGALAGV
MLASPANPTG TMIPGEQFEQ LSKWCHSHDV RIISDEIYHG ITFTDSIGDC ALQFNDDAIV
ISSFSKYWGM TGWRLGWAVL PENLVDTIAG LAGNYALCAP VPAQHAAIEA FSESAYAEGE
EALARFARAR QNVLDAAPSL GWRDLAPADG AFYMYGLVED VLGPYETATQ WCSALLETEG
VAVSPGLDFD NVNGDKWVRI SLAAGPEAVA EALRRIAKFQ AAYLTD
//
