ID A0A553L5N9_9ALTE Unreviewed; 277 AA.
AC A0A553L5N9;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=aminodeoxychorismate lyase {ECO:0000256|ARBA:ARBA00035676};
DE EC=4.1.3.38 {ECO:0000256|ARBA:ARBA00035676};
GN Name=pabC {ECO:0000313|EMBL:TRY32343.1};
GN ORFNames=FM019_05725 {ECO:0000313|EMBL:TRY32343.1};
OS Aliiglaciecola sp. M165.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Aliiglaciecola.
OX NCBI_TaxID=2593649 {ECO:0000313|EMBL:TRY32343.1, ECO:0000313|Proteomes:UP000317204};
RN [1] {ECO:0000313|EMBL:TRY32343.1, ECO:0000313|Proteomes:UP000317204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M165 {ECO:0000313|EMBL:TRY32343.1,
RC ECO:0000313|Proteomes:UP000317204};
RA Meng X.;
RT "The draft genome seqence of M165.";
RL Submitted (JUL-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:TRY32343.1}.
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DR EMBL; VKKH01000003; TRY32343.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A553L5N9; -.
DR OrthoDB; 9805628at2; -.
DR Proteomes; UP000317204; Unassembled WGS sequence.
DR GO; GO:0008696; F:4-amino-4-deoxychorismate lyase 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:SF2; AMINODEOXYCHORISMATE LYASE; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:TRY32343.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000317204}.
SQ SEQUENCE 277 AA; 30773 MW; 6A155E11A8F69293 CRC64;
MIKMVDDQTM LPINERIANY GDGCFTTIAV VKGRAELLDQ HINRLQTACE RLQIDFSDWH
SLRSAIEQKA EVLTNNVIKV LLSRGTGGRG YGTKQVSSAN CYVSISAFPS DYAKKQVNGI
TLGLCNVCLA AQPMLAGIKH VNRLEQVLAK IELEKTQFDD LLVCDSSGNV IETTAANVFF
GHQGQWVTPE LSECGIEGVM RNHIIKIMNK NNVVVHEKPI PFSQLMHFDS AFVCNSLMKL
IPISTIQLSA DNRLAFSSSH IFIDWFKDNQ NEVSINA
//
