PABC_ECOLI
ID PABC_ECOLI Reviewed; 269 AA.
AC P28305;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Aminodeoxychorismate lyase;
DE EC=4.1.3.38;
DE AltName: Full=4-amino-4-deoxychorismate lyase;
DE Short=ADC lyase;
DE Short=ADCL;
GN Name=pabC; OrderedLocusNames=b1096, JW1082;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-21, FUNCTION,
RP DISRUPTION PHENOTYPE, SUBUNIT, AND COFACTOR.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=1644759; DOI=10.1128/jb.174.16.5317-5323.1992;
RA Green J.M., Merkel W.K., Nichols B.P.;
RT "Characterization and sequence of Escherichia coli pabC, the gene encoding
RT aminodeoxychorismate lyase, a pyridoxal phosphate-containing enzyme.";
RL J. Bacteriol. 174:5317-5323(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-21.
RX PubMed=2071583; DOI=10.1016/s0021-9258(18)98790-9;
RA Green J.M., Nichols B.P.;
RT "p-aminobenzoate biosynthesis in Escherichia coli. Purification of
RT aminodeoxychorismate lyase and cloning of pabC.";
RL J. Biol. Chem. 266:12971-12975(1991).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=2251281; DOI=10.1073/pnas.87.23.9391;
RA Ye Q.-Z., Liu J., Walsh C.T.;
RT "p-aminobenzoate synthesis in Escherichia coli: purification and
RT characterization of PabB as aminodeoxychorismate synthase and enzyme X as
RT aminodeoxychorismate lyase.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9391-9395(1990).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP COFACTOR, AND SUBUNIT.
RX PubMed=10876155; DOI=10.1093/oxfordjournals.jbchem.a022727;
RA Nakai T., Mizutani H., Miyahara I., Hirotsu K., Takeda S., Jhee K.-H.,
RA Yoshimura T., Esaki N.;
RT "Three-dimensional structure of 4-amino-4-deoxychorismate lyase from
RT Escherichia coli.";
RL J. Biochem. 128:29-38(2000).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP COFACTOR, AND SUBUNIT.
RX PubMed=11841211; DOI=10.1021/bi015791b;
RA Parsons J.F., Jensen P.Y., Pachikara A.S., Howard A.J., Eisenstein E.,
RA Ladner J.E.;
RT "Structure of Escherichia coli aminodeoxychorismate synthase: architectural
RT conservation and diversity in chorismate-utilizing enzymes.";
RL Biochemistry 41:2198-2208(2002).
CC -!- FUNCTION: Involved in the biosynthesis of p-aminobenzoate (PABA), a
CC precursor of tetrahydrofolate. Converts 4-amino-4-deoxychorismate into
CC 4-aminobenzoate (PABA) and pyruvate. {ECO:0000269|PubMed:1644759,
CC ECO:0000269|PubMed:2251281}.
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:0000269|PubMed:2251281};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:10876155, ECO:0000269|PubMed:11841211,
CC ECO:0000269|PubMed:1644759};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-
CC aminobenzoate from chorismate: step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10876155,
CC ECO:0000269|PubMed:11841211, ECO:0000269|PubMed:1644759,
CC ECO:0000269|PubMed:2251281}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to produce
CC PABA. {ECO:0000269|PubMed:1644759}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; M93135; AAA24267.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74180.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35904.1; -; Genomic_DNA.
DR PIR; A42954; A42954.
DR RefSeq; NP_415614.1; NC_000913.3.
DR RefSeq; WP_000478681.1; NZ_SSZK01000019.1.
DR PDB; 1ET0; X-ray; 2.20 A; A=1-269.
DR PDB; 1I2K; X-ray; 1.79 A; A=1-269.
DR PDB; 1I2L; X-ray; 2.30 A; A=1-269.
DR PDBsum; 1ET0; -.
DR PDBsum; 1I2K; -.
DR PDBsum; 1I2L; -.
DR AlphaFoldDB; P28305; -.
DR SMR; P28305; -.
DR BioGRID; 4259420; 470.
DR BioGRID; 850991; 3.
DR DIP; DIP-10435N; -.
DR IntAct; P28305; 9.
DR STRING; 511145.b1096; -.
DR BindingDB; P28305; -.
DR ChEMBL; CHEMBL1075099; -.
DR DrugBank; DB02038; D-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-N,O-cycloserylamide.
DR jPOST; P28305; -.
DR PaxDb; P28305; -.
DR PRIDE; P28305; -.
DR EnsemblBacteria; AAC74180; AAC74180; b1096.
DR EnsemblBacteria; BAA35904; BAA35904; BAA35904.
DR GeneID; 946647; -.
DR KEGG; ecj:JW1082; -.
DR KEGG; eco:b1096; -.
DR PATRIC; fig|1411691.4.peg.1172; -.
DR EchoBASE; EB1456; -.
DR eggNOG; COG0115; Bacteria.
DR HOGENOM; CLU_020844_2_1_6; -.
DR InParanoid; P28305; -.
DR OMA; VPWTRNE; -.
DR PhylomeDB; P28305; -.
DR BioCyc; EcoCyc:ADCLY-MON; -.
DR BioCyc; MetaCyc:ADCLY-MON; -.
DR BRENDA; 4.1.3.38; 2026.
DR UniPathway; UPA00077; UER00150.
DR EvolutionaryTrace; P28305; -.
DR PRO; PR:P28305; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008696; F:4-amino-4-deoxychorismate lyase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IBA:GO_Central.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008153; P:para-aminobenzoic acid biosynthetic process; IMP:EcoCyc.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01559; ADCL_like; 1.
DR Gene3D; 3.20.10.10; -; 1.
DR Gene3D; 3.30.470.10; -; 1.
DR InterPro; IPR017824; Aminodeoxychorismate_lyase_IV.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR018300; Aminotrans_IV_CS.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR Pfam; PF01063; Aminotran_4; 1.
DR SUPFAM; SSF56752; SSF56752; 1.
DR TIGRFAMs; TIGR03461; pabC_Proteo; 1.
DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Folate biosynthesis; Lyase;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..269
FT /note="Aminodeoxychorismate lyase"
FT /id="PRO_0000103305"
FT MOD_RES 140
FT /note="N6-(pyridoxal phosphate)lysine"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:1I2K"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:1I2K"
FT HELIX 17..21
FT /evidence="ECO:0007829|PDB:1I2K"
FT STRAND 24..32
FT /evidence="ECO:0007829|PDB:1I2K"
FT HELIX 39..52
FT /evidence="ECO:0007829|PDB:1I2K"
FT HELIX 60..74
FT /evidence="ECO:0007829|PDB:1I2K"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:1I2K"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:1I2K"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:1I2K"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:1I2K"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:1I2K"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:1I2K"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:1ET0"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:1I2K"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:1I2K"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:1I2K"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:1I2K"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:1I2K"
FT HELIX 200..211
FT /evidence="ECO:0007829|PDB:1I2K"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:1I2K"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:1I2K"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:1I2K"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:1I2K"
FT STRAND 241..247
FT /evidence="ECO:0007829|PDB:1I2K"
FT HELIX 256..266
FT /evidence="ECO:0007829|PDB:1I2K"
SQ SEQUENCE 269 AA; 29715 MW; 4BC186083F5E999E CRC64;
MFLINGHKQE SLAVSDRATQ FGDGCFTTAR VIDGKVSLLS AHIQRLQDAC QRLMISCDFW
PQLEQEMKTL AAEQQNGVLK VVISRGSGGR GYSTLNSGPA TRILSVTAYP AHYDRLRNEG
ITLALSPVRL GRNPHLAGIK HLNRLEQVLI RSHLEQTNAD EALVLDSEGW VTECCAANLF
WRKGNVVYTP RLDQAGVNGI MRQFCIRLLA QSSYQLVEVQ ASLEESLQAD EMVICNALMP
VMPVCACGDV SFSSATLYEY LAPLCERPN
