ID D2EP25_9STRE Unreviewed; 380 AA.
AC D2EP25;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=Aminotransferase, class V {ECO:0000313|EMBL:EFA24839.1};
GN ORFNames=HMPREF0850_00713 {ECO:0000313|EMBL:EFA24839.1};
OS Streptococcus sp. M143.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=563037 {ECO:0000313|EMBL:EFA24839.1, ECO:0000313|Proteomes:UP000002766};
RN [1] {ECO:0000313|EMBL:EFA24839.1, ECO:0000313|Proteomes:UP000002766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M143 {ECO:0000313|EMBL:EFA24839.1,
RC ECO:0000313|Proteomes:UP000002766};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Sibley C.D., Field T.R., Grinwis M., Eshaghurshan C.S.,
RA Surette M.G., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Streptococcus sp. strain M143.";
RL Submitted (OCT-2009) 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:RU004504};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily.
CC {ECO:0000256|ARBA:ARBA00006490}.
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DR EMBL; GG730097; EFA24839.1; -; Genomic_DNA.
DR RefSeq; WP_000638931.1; NZ_GG730097.1.
DR AlphaFoldDB; D2EP25; -.
DR eggNOG; COG1104; Bacteria.
DR HOGENOM; CLU_003433_0_0_9; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000002766; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.260.50; -; 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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR016454; Cysteine_dSase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11601:SF50; CYSTEINE DESULFURASE ISCS 2-RELATED; 1.
DR PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EFA24839.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000313|EMBL:EFA24839.1}.
FT DOMAIN 2..365
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 380 AA; 41692 MW; 141C48B3335204FA CRC64;
MIYFDNSATT KPYPEALETY MQVASKIVGN PSSLHRLGDQ ATRILDASRQ QIADLIGKKS
DEIFFTSGGT EGDNWVIKGV AFEKAQFGKH IIVSAIEHPA VKESALWLKS QGFEIDFAPV
DEKGFVDVEA LANLIRPDTI LVSIMAVNNE IGSIQPIETI SELLADKPTI SFHVDAVQAL
AKIPTEKYLT DRVDFATFSS HKFHGVRGVG FVYIKSGKKI TPLLTGGGQE HDYRSTTENV
AGIAATAKAL RLSMEKLAIF ASKTGQMRSV IRQALLDYPD ILIFSDEEDF APHILTFGIK
GVRGEVIVHA FEDYDIFIST TSACSSKAGK PAGSLLAMGV DKDKAQSAVR LSLDLENDMS
QVEQFLTKLK LIYNQTRKVR
//