ID A0A101WKQ6_9FIRM Unreviewed; 380 AA.
AC A0A101WKQ6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=UDP-4-amino-4, 6-dideoxy-N-acetyl-beta-L-altrosamine transaminase {ECO:0000313|EMBL:KUO74799.1};
GN ORFNames=APF77_11095 {ECO:0000313|EMBL:KUO74799.1};
OS Clostridia bacterium BRH_c25.
OC Bacteria; Bacillota; Clostridia.
OX NCBI_TaxID=1734399 {ECO:0000313|EMBL:KUO74799.1, ECO:0000313|Proteomes:UP000057710};
RN [1] {ECO:0000313|EMBL:KUO74799.1, ECO:0000313|Proteomes:UP000057710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c25 {ECO:0000313|EMBL:KUO74799.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) 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:KUO74799.1}.
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DR EMBL; LOES01000083; KUO74799.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101WKQ6; -.
DR STRING; 1734399.APF77_11095; -.
DR Proteomes; UP000057710; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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; IPR020026; PseC.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR03588; PseC; 1.
DR PANTHER; PTHR30244:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 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 Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}.
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 183
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 380 AA; 42482 MW; 497D809A798EC2D4 CRC64;
MRKFIPYGKQ YIDEEDIQAV VEVLKSDYIT TGPKIEELEN SITEFTGAKY AVAVSNGTAA
LHAACFAAGI GPGDEVITTP MTFAASANCV LYMGADPVFA DIDPETYNID PQAIERKITD
RTRAIIPVHF TGQPCDMDAI MKIAEKYGLA VIEDGAHALG AVYKNRKIGT LGSMTTFSFH
PVKQITTGEG GAVTTNDSSL YDKLLMFRTH GITRDAEKME SNEGPWFYEQ QYLGFNYRMT
DIQAALGISQ MKKLDSFLEK RRSYAALYNK LLGGLEGVTV PYQAEDVSSA WHLYIVKLNL
GKLALGRREV FEKLRDKNIG VNVHYIPVYY HSYYKEIGYG KGLCPETEAL YEAIITLPLY
PTMEIDDIHY IVDNFKDIIR
//
