ID E8LHW1_SUCHY Unreviewed; 418 AA.
AC E8LHW1;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Aminotransferase, class III {ECO:0000313|EMBL:EFY07899.1};
GN ORFNames=HMPREF9444_00274 {ECO:0000313|EMBL:EFY07899.1};
OS Succinatimonas hippei (strain DSM 22608 / JCM 16073 / KCTC 15190 / YIT
OS 12066).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Succinivibrionaceae; Succinatimonas.
OX NCBI_TaxID=762983 {ECO:0000313|EMBL:EFY07899.1, ECO:0000313|Proteomes:UP000018458};
RN [1] {ECO:0000313|EMBL:EFY07899.1, ECO:0000313|Proteomes:UP000018458}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22608 / JCM 16073 / KCTC 15190 / YIT 12066
RC {ECO:0000313|Proteomes:UP000018458};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-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 -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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:EFY07899.1}.
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DR EMBL; AEVO01000010; EFY07899.1; -; Genomic_DNA.
DR RefSeq; WP_009142499.1; NZ_GL830948.1.
DR AlphaFoldDB; E8LHW1; -.
DR STRING; 762983.HMPREF9444_00274; -.
DR GeneID; 78338863; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_6; -.
DR OrthoDB; 3398487at2; -.
DR Proteomes; UP000018458; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00610; OAT_like; 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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 3.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:EFY07899.1}; Coiled coil {ECO:0000256|SAM:Coils};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000018458};
KW Transferase {ECO:0000313|EMBL:EFY07899.1}.
FT COILED 312..339
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 418 AA; 46471 MW; 936B568C218E4E1C CRC64;
MNKIVEKYLA ADRELIAPVQ HIAELPLVVK NAEGPYLISA ENKRYLDFTS GACTMSLGYG
IKNDNEFGSF PFPYASGVNQ IEYAKKLTKK FPGGFLSQIA FSVCGSDTND AAIKFSRAYT
GRQKIVTFEG DYHGTTFGAA SLTTLPGRLS NKFAPMVGEI YSVPFCDEYA DDGQIDAVIE
KIKALDCNTI AGFIVEPIQG DMGMLPMHQR LMHEIYSLSR KHHCAFIADE VQMAFYRTGP
FFSIENYPDV FPDAVTMGKH IGGGIPLGAI LGRKDFMQAL GPCEHAFSMA GNSEACARGL
YNFNLIESKD FQDNLHKNIE ILQNELNSLQ LKYPSVIEKY TGIGLAYGLW VKSISSSEDD
NEACKKIIKR AFDLGLYTMR IGSNWIRIEP MLNLDEKLLK EGMAILDRAV ADYSEHRI
//
