ID G2PUK8_9FIRM Unreviewed; 387 AA.
AC G2PUK8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Aminotransferase class V {ECO:0000313|EMBL:AEM74481.1};
GN ORFNames=Calla_1907 {ECO:0000313|EMBL:AEM74481.1};
OS Caldicellulosiruptor acetigenus 6A.
OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX NCBI_TaxID=632516 {ECO:0000313|EMBL:AEM74481.1, ECO:0000313|Proteomes:UP000009257};
RN [1] {ECO:0000313|EMBL:AEM74481.1, ECO:0000313|Proteomes:UP000009257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6A {ECO:0000313|EMBL:AEM74481.1,
RC ECO:0000313|Proteomes:UP000009257};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Blumer-Schuette S.E.,
RA Kelly R.M., Woyke T.;
RT "Complete sequence of Caldicellulosiruptor lactoaceticus 6A.";
RL Submitted (AUG-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|PIRSR:PIRSR000524-50, ECO:0000256|RuleBase:RU004504};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236,
CC ECO:0000256|RuleBase:RU004075}.
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DR EMBL; CP003001; AEM74481.1; -; Genomic_DNA.
DR RefSeq; WP_014043034.1; NC_015949.1.
DR AlphaFoldDB; G2PUK8; -.
DR KEGG; clc:Calla_1907; -.
DR HOGENOM; CLU_027686_1_1_9; -.
DR Proteomes; UP000009257; Chromosome.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 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:AEM74481.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Transferase {ECO:0000313|EMBL:AEM74481.1}.
FT DOMAIN 7..331
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 191
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 387 AA; 43048 MW; 62FEC976C76F3EF9 CRC64;
MRKPKLLMTP GPTPLPPEVI AAMSQQIIHH RTKEFGEIFS RVNENLKKVF QTKNNVLTFA
ASGTGAMEAS AVNFFSEGDT VLVVSVGVFG DRFINICKTF GLNVIEKKYP YGDVANIDEV
IEIIESNKDI KGVFITHNET STGVTNPIEK LARYLKNTDK ILIVDAVSSL GAIDLKTDEW
GVDVVVTGSH KALMSPPGLA FVSVSEKAWG FYKKSQLRKF YWDLKKYQDN LLKESQDTPF
TPAVTLIRAV DVGLKLILDY GLENNFKRHT RLAHLTQLAA EKLNLELLPK KEYSSAVITA
IKSPEGVDIE KVRKIMNQKY DIMVTGGQST LKGKIIRIGH MGYVDEFDLL KTIECFELAL
LEVGYKNFEV GEATKAVLQE IAKGVNS
//
