ID A0A1F3P1V9_9BACT Unreviewed; 368 AA.
AC A0A1F3P1V9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Cell wall biogenesis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A3G23_12260 {ECO:0000313|EMBL:OFY70887.1};
OS Bacteroidetes bacterium RIFCSPLOWO2_12_FULL_37_12.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797365 {ECO:0000313|EMBL:OFY70887.1, ECO:0000313|Proteomes:UP000176497};
RN [1] {ECO:0000313|EMBL:OFY70887.1, ECO:0000313|Proteomes:UP000176497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OFY70887.1}.
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DR EMBL; MEPC01000020; OFY70887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3P1V9; -.
DR STRING; 1797365.A3G23_12260; -.
DR Proteomes; UP000176497; Unassembled WGS sequence.
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 Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}.
FT ACT_SITE 187
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 187
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 368 AA; 41451 MW; D92C62307C98F975 CRC64;
MKYFVPFVNP AANYLLIKNE LETVYHEIMS KGDLVYRHQL KSFEDNLAKF VGTKYAVGLN
SGYDALHLSL RAAGIGKGDE VMVPAHTFVA TCSAIVNVGA TPVLVDVGKD FNIDIIQIEK
AITPRTKGII PVHLNGFMAD MPVIEKIAEK HNLVIVEDAC QSLGSFIHGK KAGAWGLTGC
FSFYPFKILG GYGDGGAITT NNESVALFVK RMRYNGEDRE TGEYHGHGFT CILDNLQAGF
LDLKLKFFPE WIKIRKSIAE KYWKAFSEIP DLFLPHYSKP GFDHVYQNYV VRAKQGNEFS
EYLKKNGVEV LTQFRKPYYK HTELNLIDRG FPETEQLSKE VCSLPMCVEL TEEQIAYVIK
VVRGFYGK
//
