ID G4CMD0_9NEIS Unreviewed; 868 AA.
AC G4CMD0;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN Name=acnD {ECO:0000313|EMBL:EGZ51210.1};
GN ORFNames=HMPREF9370_0239 {ECO:0000313|EMBL:EGZ51210.1};
OS Neisseria wadsworthii 9715.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=1030841 {ECO:0000313|EMBL:EGZ51210.1, ECO:0000313|Proteomes:UP000005336};
RN [1] {ECO:0000313|EMBL:EGZ51210.1, ECO:0000313|Proteomes:UP000005336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9715 {ECO:0000313|EMBL:EGZ51210.1,
RC ECO:0000313|Proteomes:UP000005336};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336,
CC ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00023501};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
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:EGZ51210.1}.
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; AGAZ01000008; EGZ51210.1; -; Genomic_DNA.
DR RefSeq; WP_009115386.1; NZ_JH165159.1.
DR AlphaFoldDB; G4CMD0; -.
DR STRING; 1030841.HMPREF9370_0239; -.
DR PATRIC; fig|1030841.3.peg.247; -.
DR HOGENOM; CLU_013476_2_1_4; -.
DR OrthoDB; 9764318at2; -.
DR Proteomes; UP000005336; Unassembled WGS sequence.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IEA:InterPro.
DR Gene3D; 6.10.190.10; -; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR InterPro; IPR012708; 2Me_IsoCit_deHydtase_FeS-dep.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR006249; Aconitase/IRP2.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR02333; 2met_isocit_dHY; 1.
DR PANTHER; PTHR11670:SF43; 2-METHYLCITRATE DEHYDRATASE (2-METHYL-TRANS-ACONITATE FORMING); 1.
DR PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000313|EMBL:EGZ51210.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 62..539
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 661..793
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 868 AA; 95536 MW; A1BF7939D4198489 CRC64;
MKTNQIYRKP LPDTNLEYYD ARAACEDIKP GSYDTLPYTS RILAENLVNR ADNVDLPTLQ
SWLRQLIERK QEIDFPWFPA RVVCHDILGQ TALVDLAGLR DAIAEKGGDP SKVNPVVQTQ
LIVDHSLAVE CGGYDPDAFR KNREIEDRRN EDRFHFINWT KTAFENVDVI PAGNGIMHQI
NLEKMSPVIQ VRNGVAFPDT CVGTDSHTPH VDALGVISVG VGGLEAETVM LGRASMMRLP
DIVGVELTGK RQPGITATDI VLALTEFLRK ERVVGAFVEF FGEGARSLSI GDRATISNMT
PEFGATAAMF SIDEQTIDYL KLTGRDDEQV KLVENYAKTA GLWSDALAKA EYPRVLKFDL
STVTRNMAGP SNPHARFSTT DLAAKGIAAP YEEPSDGKMP DGAVIIAAIT SCTNTSNPRN
VVAAALLARN ANKLGLTRKP WVKSSFAPGS KVAEIYLKEA GLLPELEQLG FGIVAFACTT
CNGMSGALDP KIQQEIIDRD LYATAVLSGN RNFDGRIHPY AKQAFLASPP LVVAYAIAGS
IRFDIENDVL GVSDGKEIRL KDIWPTDEEI DEIVAKHVKP QQFRDVYIPM FDTGTAEKAP
SPLYDWRPMS TYIRRPPYWE GALAGERTLK GMRPLAILPD NITTDHLSPS NAILPTSAAG
EYLAKMGLPE EDFNSYATHR GDHLTAQRAT FANPKLFNEM VKNEDGTTKQ GSLARVEPEG
QVMRMWEAIE TYMNRKQPLI IVAGADYGQG SSRDWAAKGV RLAGVEAIVA EGFERIHRTN
LIGMGVLPLQ FKEGVNRHTL ELDGTETYDV IGKREPRCDL TLVIHRKNGE TVEVPVTCRL
DTAEEVLIYE AGGVLQRFAQ DFLEGNAA
//
