ID F9HGF7_9STRE Unreviewed; 353 AA.
AC F9HGF7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Aminotransferase, class V {ECO:0000313|EMBL:EGP66335.1};
GN ORFNames=HMPREF9182_0384 {ECO:0000313|EMBL:EGP66335.1};
OS Streptococcus sp. oral taxon 056 str. F0418.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=904294 {ECO:0000313|EMBL:EGP66335.1, ECO:0000313|Proteomes:UP000004514};
RN [1] {ECO:0000313|Proteomes:UP000004514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0418 {ECO:0000313|Proteomes:UP000004514};
RA Durkin A.S., Kim M., Radune D., Hostetler J., Torralba M., Gillis M.,
RA Methe B., Sutton G., Nelson K.E.;
RT "Complete sequence of Bifidobacterium breves ACS-071-V-Sch8b.";
RL Submitted (MAY-2011) 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}.
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:EGP66335.1}.
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DR EMBL; AFQU01000001; EGP66335.1; -; Genomic_DNA.
DR AlphaFoldDB; F9HGF7; -.
DR eggNOG; COG1104; Bacteria.
DR Proteomes; UP000004514; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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:EGP66335.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000004514};
KW Transferase {ECO:0000313|EMBL:EGP66335.1}.
FT DOMAIN 38..338
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 353 AA; 38881 MW; D87A4F93853CCC5D CRC64;
MGKSIQSAQF RQSGNPPFRS FTPSNSRAFR QVFVRDFFTS GGTEGDNWVL KGVAFEKIPF
GKHIIVSSIE HPAVKESALW LQSQGFEIDF APVDKAGFVD VDELANLIRP DTTLVSIMAV
NNEIGSLQPI QKISELLADK PTISFHVDAV QAVTKIPTAS YLTDRVDFAT FSSHKFHGVR
GVGFVYIKSG KKISPLLTGG GQESDKRSTT ENLAGIAATA KALRLSMEKQ EAFAQRTAQM
KQILLEELQK YPDVVIFSDI EDFAPHILTF GIKGVRGEVV VHAFEDYEIY ISTTSACSSK
AGKPAGTLIA MGVEKSLAQT AVRISLDLDN DMSQMEQFLT TFKIIYEKTR KVR
//
