ID E6KUQ0_9ACTO Unreviewed; 366 AA.
AC E6KUQ0;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Pyridoxal-phosphate-dependent aminotransferase {ECO:0000313|EMBL:EFU60469.1};
DE EC=2.6.1.50 {ECO:0000313|EMBL:EFU60469.1};
GN Name=stsC {ECO:0000313|EMBL:EFU60469.1};
GN ORFNames=HMPREF9006_1952 {ECO:0000313|EMBL:EFU60469.1};
OS Actinomyces sp. oral taxon 180 str. F0310.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=888052 {ECO:0000313|EMBL:EFU60469.1, ECO:0000313|Proteomes:UP000006252};
RN [1] {ECO:0000313|EMBL:EFU60469.1, ECO:0000313|Proteomes:UP000006252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0310 {ECO:0000313|EMBL:EFU60469.1,
RC ECO:0000313|Proteomes:UP000006252};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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:EFU60469.1}.
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DR EMBL; AEPP01000036; EFU60469.1; -; Genomic_DNA.
DR RefSeq; WP_009213391.1; NZ_GL622194.1.
DR AlphaFoldDB; E6KUQ0; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_7_2_11; -.
DR OrthoDB; 9804264at2; -.
DR Proteomes; UP000006252; Unassembled WGS sequence.
DR GO; GO:0047310; F:glutamine-scyllo-inositol transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0080100; F:L-glutamine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EFU60469.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:EFU60469.1}.
FT ACT_SITE 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 185
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 366 AA; 38911 MW; 732FC8E3A56AA1A7 CRC64;
MTPSFIPPAR PLIGEEEISA VARVMRTGMI AQGPQVEAFE EEFARQIVPG TRAIALNSGT
SALHLGLLAA GIGPGDEVIV PSFTFAATAN AVAITGATPV FADIDPRTFT LSPASVSSAV
SARTRAIMPV HLYGHPAALD TLDAIARERG LLLFEDAAQA HGASLHGRPV GSFGTFAAFS
FYPTKNMTSG EGGMVTSRDP ALVRWVRLAR NQGMEKRYEN EIVGLNNRMT DIHAAIGRVQ
LTKIDAWTAE RQSNAAYLSA HLRGVTVPHV APGATHVFHQ YTIRVPQDRD GFARALREEY
GIGSGVYYPI PAHELASLAR FAPDTDLPAT RAAAAEVLSL PVYPSLTRGD LDRIVEAVNA
LAEAGA
//