ID Q4JT60_CORJK Unreviewed; 1172 AA.
AC Q4JT60;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=isochorismate synthase {ECO:0000256|ARBA:ARBA00012824};
DE EC=5.4.4.2 {ECO:0000256|ARBA:ARBA00012824};
GN Name=dhbE {ECO:0000313|EMBL:CAI37997.1};
GN OrderedLocusNames=jk1820 {ECO:0000313|EMBL:CAI37997.1};
OS Corynebacterium jeikeium (strain K411).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=306537 {ECO:0000313|EMBL:CAI37997.1, ECO:0000313|Proteomes:UP000000545};
RN [1] {ECO:0000313|EMBL:CAI37997.1, ECO:0000313|Proteomes:UP000000545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K411 {ECO:0000313|EMBL:CAI37997.1,
RC ECO:0000313|Proteomes:UP000000545};
RX PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005;
RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT "Complete genome sequence and analysis of the multiresistant nosocomial
RT pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT human skin flora.";
RL J. Bacteriol. 187:4671-4682(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate = isochorismate; Xref=Rhea:RHEA:18985,
CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29780; EC=5.4.4.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000799};
CC -!- SIMILARITY: Belongs to the isochorismate synthase family.
CC {ECO:0000256|ARBA:ARBA00005297}.
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DR EMBL; CR931997; CAI37997.1; -; Genomic_DNA.
DR RefSeq; WP_011274158.1; NC_007164.1.
DR AlphaFoldDB; Q4JT60; -.
DR STRING; 306537.jk1820; -.
DR GeneID; 3433702; -.
DR KEGG; cjk:jk1820; -.
DR PATRIC; fig|306537.10.peg.1843; -.
DR eggNOG; COG1021; Bacteria.
DR eggNOG; COG1169; Bacteria.
DR eggNOG; COG1535; Bacteria.
DR HOGENOM; CLU_008171_0_0_11; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000000545; Chromosome.
DR GO; GO:0008908; F:isochorismatase activity; IEA:InterPro.
DR GO; GO:0008909; F:isochorismate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.60.120.10; Anthranilate synthase; 1.
DR Gene3D; 3.40.50.850; Isochorismatase-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR005801; ADC_synthase.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR015890; Chorismate_C.
DR InterPro; IPR004561; IsoChor_synthase.
DR InterPro; IPR016291; Isochorismatase.
DR InterPro; IPR000868; Isochorismatase-like.
DR InterPro; IPR036380; Isochorismatase-like_sf.
DR NCBIfam; TIGR00543; isochor_syn; 1.
DR PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR Pfam; PF00857; Isochorismatase; 1.
DR PRINTS; PR01398; ISCHRISMTASE.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF56322; ADC synthase; 1.
DR SUPFAM; SSF52499; Isochorismatase-like hydrolases; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Ligase {ECO:0000313|EMBL:CAI37997.1};
KW Nucleotidyltransferase {ECO:0000313|EMBL:CAI37997.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000545};
KW Transferase {ECO:0000313|EMBL:CAI37997.1}.
FT DOMAIN 35..206
FT /note="Isochorismatase-like"
FT /evidence="ECO:0000259|Pfam:PF00857"
FT DOMAIN 317..573
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT DOMAIN 647..1019
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 1070..1146
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT REGION 781..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1172 AA; 126932 MW; 09DABF0307CB95EC CRC64;
MAIPPISPYP IPTPSTTLPA DCPARSWALE PARAALLVHD MQKYFLAAYD WNKEPLHSAL
ANIARLITTA DQLGIPVFYS AQPPQQHPTR RGLLSDMWGQ GLQTAEEASI IKELAPGKHH
QILTKWRYSA FERTDLYQSL AFARRDQLII TGVYGHMGCK VTAVDAFMKD IQPFVITDGI
ADFTAQDHQE TIDWVAKRCG RSLDTASALK QLEVHDGPPS GEASGPPSFV MSDSDQTLTT
CGVKTRYGTV EQAAAALRRA AEAGREDVVV GALPFDPDTA PVLLAPESFQ RHAGAPRWKT
APLVPDVVDI SQRPSLQEHG RRVSRAVEAI GRGKFQKVVL SREEEYTLAS PVEPEALLRG
FMETSATGHG HLVATTNGPE EAFFVGSSPE LLIRKEGARI VSHPLAGTIA RSEDPVTDWA
RAIELTLSHK DIAEHRFVTT AIRKVLEPLC TQLHVPELPT LTATSHTWHL GTHIEGTLRN
PDTSVLELAA LLHPTPAVNG APSAAALDFL RQQEPERGLY GGAIGYADSH GDGEWRVAIR
SATVQGSQVS ARAGGGIVAE SQPDQEIEET NFKLGPVRAL LGLAAKGDTE GTAQPPSAHI
APNPEPHLSP LNGSHGPEVL ANHMPRTLAQ EYHRQGIWTH HTHWDVFQQT VATFPNRPAT
TDGHRSLSWH ELDNSVETAA HYLHQAGVRR GDGCILQLPN SVVFLETLLA LWKLGAIPIF
ALPDLGSTEV RHFASHAPAR FYISTSRPDR HLAGVHATLQ EPLDDGRTVR AILIDETAES
PWATESTGHS EAANEESPAP PTADVEADEL AFLQLSGGTT GLPKLIPRTH ADYLYSIRCA
LQACDLETES CLLVALPAAH NFTLSSPGIL GALLRGAHIV FAKSPMPSDL LPAIDHHGAT
HLALVPPAVL GILNAPARDR HDLRTLRTLW VGGAKLSAEV ARRIRPELDC QLQQVFGMAE
GLVNFTPLNA STEEIINTQG RPMSSHDEIC IVDDATLPLP EGHPGHLLTR GPYTIRGYHR
AEEINSRAFT EDGFYITGDI VTVDDSALTV VGRAKDQINR GGEKVAPEAV ENALLSHPDI
HDVSVVGTPD DNLGEAITAY VILRDGVDDL TPLAVRKHAR AAGIARFAVP DHVHIVEEFP
TTGVGKVNKR IQQNNADSTA ERKAERKIEV AN
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