GenomeNet

Database: UniProt
Entry: A0A5C6DE54_9BACT
LinkDB: A0A5C6DE54_9BACT
Original site: A0A5C6DE54_9BACT 
ID   A0A5C6DE54_9BACT        Unreviewed;       288 AA.
AC   A0A5C6DE54;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   RecName: Full=aminodeoxychorismate lyase {ECO:0000256|ARBA:ARBA00035676};
DE            EC=4.1.3.38 {ECO:0000256|ARBA:ARBA00035676};
GN   Name=dat {ECO:0000313|EMBL:TWU34077.1};
GN   ORFNames=S225a_13350 {ECO:0000313|EMBL:TWU34077.1};
OS   Candidatus Brocadiaceae bacterium S225.
OC   Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC   Candidatus Brocadiaceae.
OX   NCBI_TaxID=2528033 {ECO:0000313|EMBL:TWU34077.1, ECO:0000313|Proteomes:UP000315241};
RN   [1] {ECO:0000313|EMBL:TWU34077.1, ECO:0000313|Proteomes:UP000315241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S225 {ECO:0000313|EMBL:TWU34077.1,
RC   ECO:0000313|Proteomes:UP000315241};
RA   Wiegand S., Jogler M., Boedeker C., Pinto D., Vollmers J., Rivas-Marin E.,
RA   Kohn T., Peeters S.H., Heuer A., Rast P., Oberbeckmann S., Bunk B.,
RA   Jeske O., Meyerdierks A., Storesund J.E., Kallscheuer N., Luecker S.,
RA   Lage O.M., Pohl T., Merkel B.J., Hornburger P., Mueller R.-W., Bruemmer F.,
RA   Labrenz M., Spormann A.M., Op Den Camp H., Overmann J., Amann R.,
RA   Jetten M.S.M., Mascher T., Medema M.H., Devos D.P., Kaster A.-K.,
RA   Ovreas L., Rohde M., Galperin M.Y., Jogler C.;
RT   "Deep-cultivation of Planctomycetes and their phenomic and genomic
RT   characterization uncovers novel biology.";
RL   Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-amino-4-deoxychorismate = 4-aminobenzoate + H(+) + pyruvate;
CC         Xref=Rhea:RHEA:16201, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17836, ChEBI:CHEBI:58406; EC=4.1.3.38;
CC         Evidence={ECO:0000256|ARBA:ARBA00035576};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-
CC       aminobenzoate from chorismate: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00035633}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009320}.
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:TWU34077.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; SMSL01000006; TWU34077.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C6DE54; -.
DR   Proteomes; UP000315241; Unassembled WGS sequence.
DR   GO; GO:0008696; F:4-amino-4-deoxychorismate lyase activity; IEA:InterPro.
DR   GO; GO:0047810; F:D-alanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.470.10; -; 1.
DR   Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 1.
DR   InterPro; IPR017824; Aminodeoxychorismate_lyase_IV.
DR   InterPro; IPR001544; Aminotrans_IV.
DR   InterPro; IPR036038; Aminotransferase-like.
DR   InterPro; IPR043132; BCAT-like_C.
DR   InterPro; IPR043131; BCAT-like_N.
DR   NCBIfam; TIGR03461; pabC_Proteo; 1.
DR   PANTHER; PTHR42743; AMINO-ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42743:SF20; BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE-LIKE PROTEIN 2; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:TWU34077.1};
KW   Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000315241};
KW   Transferase {ECO:0000313|EMBL:TWU34077.1}.
SQ   SEQUENCE   288 AA;  32458 MW;  306BA6DF57A85229 CRC64;
     MHSISIMTKF IFLNGRIIPD TEGSVSTDDR GFLYGDGIYE TLRSYDGKPF KLAEHLERMR
     HSAKQLRILF EYTNTEISEI IKTLIDKNNI QDAYIRITLS RGAGGGRLQM DDNIEPTTLI
     QVKPFSPYDS KLYDEGMTLV VSDYRRSTTC PISHYKTTNL LKSILLKEEA KTKSAHEAII
     LNTDSYVAEC VVSNIFMVSG GSVITPSLDT NILPGITRIT VLDICKNKSI PISENHFTTD
     RLIKANEVFI TNSLMEIMPV SKIDNYKIGK VIPGMITQQV MSAYKRLI
//
DBGET integrated database retrieval system