ID C5NY00_9BACL Unreviewed; 524 AA.
AC C5NY00;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Aminotransferase, class V {ECO:0000313|EMBL:EER67682.1};
GN ORFNames=GEMHA0001_0335 {ECO:0000313|EMBL:EER67682.1};
OS Gemella haemolysans ATCC 10379.
OC Bacteria; Bacillota; Bacilli; Bacillales; Gemellaceae; Gemella.
OX NCBI_TaxID=546270 {ECO:0000313|EMBL:EER67682.1, ECO:0000313|Proteomes:UP000006004};
RN [1] {ECO:0000313|EMBL:EER67682.1, ECO:0000313|Proteomes:UP000006004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10379 {ECO:0000313|EMBL:EER67682.1,
RC ECO:0000313|Proteomes:UP000006004};
RA Fulton L., Clifton S., Chinwalla A.T., Mitreva M., Sodergren E.,
RA Weinstock G., Clifton S., Dooling D.J., Fulton B., Minx P., Pepin K.H.,
RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EER67682.1, ECO:0000313|Proteomes:UP000006004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10379 {ECO:0000313|EMBL:EER67682.1,
RC ECO:0000313|Proteomes:UP000006004};
RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (JUN-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 -!- 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:EER67682.1}.
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DR EMBL; ACDZ02000014; EER67682.1; -; Genomic_DNA.
DR RefSeq; WP_003145015.1; NZ_ACDZ02000014.1.
DR AlphaFoldDB; C5NY00; -.
DR GeneID; 78010553; -.
DR eggNOG; COG0075; Bacteria.
DR OrthoDB; 389074at2; -.
DR Proteomes; UP000006004; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.630.30; -; 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; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42778; 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE; 1.
DR PANTHER; PTHR42778:SF1; 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE; 1.
DR Pfam; PF13673; Acetyltransf_10; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 4: Predicted;
KW Aminotransferase {ECO:0000313|EMBL:EER67682.1};
KW Transferase {ECO:0000313|EMBL:EER67682.1}.
FT DOMAIN 1..163
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 524 AA; 59752 MW; 4D2552EEE0E54CAF CRC64;
MIYKIANTAE EYEQIFKLNY ETFVEEIPQH EKNETKKLKD KFHDKNIYII AKKKNDVIGM
ISLSDQRPFS LDLKLNDIDK FYKGSYKKPV EIRLLSIKEQ YRKTKVFTEL LQRTFNYIIQ
NAYDIVFISG TTRQEKLYNH IGFVKFHENV GTKEAEYMPM YLRLDNGNKV IERLARAQRI
NFLPGPVDLS EDVIAKLSKQ LYSHRSSEFV ALTKDTLAKI EGILDVKQAT ILHGSATLAN
EAIMAQLKGR NLINGLVLAN GEFGNRLVRE TKRHGLNIET YSVGFGESFD LDVLSDKLKS
GNYDFVYVVH NETSVGILND LDEITRIVKD NNLVLAVDAV SAVGAIKYSY KDVDYVACSS
GKAFCSVAGL AIVGSNCELV PLENTPLYLD LHYANKLTSI PFTQPSILME ALNTALDAFK
TDERYEKVQE KYTYMKEGLK QLNLPIMKFK EKEVSPVIIT VELPESISSL NVGSSLAINN
IFIHYKSSYL QERNIIQFSF ININTTKNEI DYTLNILKQM IGDY
//
