ID F6CRS3_MARPP Unreviewed; 933 AA.
AC F6CRS3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Aconitate hydratase {ECO:0000313|EMBL:AEF54926.1};
DE EC=4.2.1.3 {ECO:0000313|EMBL:AEF54926.1};
GN OrderedLocusNames=Mar181_1888 {ECO:0000313|EMBL:AEF54926.1};
OS Marinomonas posidonica (strain CECT 7376 / NCIMB 14433 / IVIA-Po-181).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=491952 {ECO:0000313|EMBL:AEF54926.1, ECO:0000313|Proteomes:UP000009230};
RN [1] {ECO:0000313|EMBL:AEF54926.1, ECO:0000313|Proteomes:UP000009230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7376 / NCIMB 14433 / IVIA-Po-181
RC {ECO:0000313|Proteomes:UP000009230};
RX PubMed=23458837; DOI=10.4056/sigs.2976373;
RA Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA Detter J.C., Copeland A., Lu M., Bruce D., Detter C., Tapia R., Han S.,
RA Land M.L., Ivanova N., Mikhailova N., Johnston A.W., Sanchez-Amat A.;
RT "Complete genome sequence of Marinomonas posidonica type strain (IVIA-Po-
RT 181(T)).";
RL Stand. Genomic Sci. 7:31-43(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-
CC aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57429, ChEBI:CHEBI:57872; EC=4.2.1.99;
CC Evidence={ECO:0000256|ARBA:ARBA00000118};
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
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DR EMBL; CP002771; AEF54926.1; -; Genomic_DNA.
DR AlphaFoldDB; F6CRS3; -.
DR STRING; 491952.Mar181_1888; -.
DR KEGG; mpc:Mar181_1888; -.
DR eggNOG; COG1049; Bacteria.
DR HOGENOM; CLU_314657_0_0_6; -.
DR OrthoDB; 9758061at2; -.
DR Proteomes; UP000009230; Chromosome.
DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:RHEA.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 3.40.1060.10; Aconitase, Domain 2; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR Gene3D; 1.25.40.310; Aconitate B, HEAT-like domain; 1.
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; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR015933; Aconitase_B_HEAT-like_dom.
DR InterPro; IPR036288; Aconitase_B_HEAT-like_dom_sf.
DR InterPro; IPR015929; Aconitase_B_swivel.
DR InterPro; IPR015932; Aconitase_dom2.
DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR PANTHER; PTHR43160:SF4; ACONITATE HYDRATASE B; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF06434; Aconitase_2_N; 1.
DR Pfam; PF11791; Aconitase_B_N; 1.
DR SUPFAM; SSF74778; Aconitase B, N-terminal domain; 1.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000313|EMBL:AEF54926.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 6..162
FT /note="Aconitase B HEAT-like"
FT /evidence="ECO:0000259|Pfam:PF11791"
FT DOMAIN 179..405
FT /note="Aconitase B swivel"
FT /evidence="ECO:0000259|Pfam:PF06434"
FT DOMAIN 409..893
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
SQ SEQUENCE 933 AA; 100662 MW; AEA454FD71556BCC CRC64;
MSLYLEYLQE IEDRKGEGLH PKPIDGGELL TEIIAQIKDT EHEHREDSLN FFIYNSLPGT
TSAAAVKAKF LKEIILGEET VAEISAERAL EFLSHMKGGP SVEVLIDLAL ADDAKVASAA
AEVLKTQVFL YEADMERLEV AYKAGNKIAT EILESYAKAE FFTKLPDIDE KIEVITYIAG
EGDISTDLLS PGNQAHSRAD RELHGKCMIS PEAQQEIVEL KEKHPNAKVM LIAEKGTMGV
GSSRMSGVNN VALWAGKQAS PYVPFVNFAP VVAGTNGISP IFLTTVGVTG GIGIDLKNWV
KKVDANGNTV VDANGDPILE EAYSVATGTL LTIDTKKKKL YNGDKELVDL SDSFIAQKVE
FMRAGGSYAV VFGKKLQTFA AETLGVEAPQ VYAPSQEISV EGQGLTAVEK IFNNNAVGVN
SDTPLHAGSD VRVKVNIVGS QDTTGPMTAQ ELESMAASVI SPIVDGAYQS GCHTASVWDS
KAQANIPKLM SFMSNFGLIT ARDPKGVYPP MTDVIHKVLN DITIDDRAII IGGDSHTRMS
KGVAFGADSG TVALALATGE AAMPIPDSVK VTFKGHMKSH MDFRDVVHAT QAQMLKQFGG
ENVFQGRIIE VHIGTLLADQ AFTFTDWTAE MKAKASICIS TDDTLVQSLE LAKSRIQIMI
NKGMENEAKT LHGLIALADK RIAGIKSGEQ PALAPDNNAK YFAEVVVDLD EIAEPMIADP
DVNNDDVSKR YTHDVIRPVS FYNNKPVDLA FVGSCMVHKG DIQIIAQMLR NIESKQGSVS
FKAPLVVAAP TYNIVDELKA EGDWDILTKY AGFEFDDSNP KGQARTKYEN ILYLERPGCN
LCMGNQEKAE PGDTVIATST RLFQGRVVAD SSEKKGESLL GSTPLVVLSA VLGRFPSMDE
YLSAVDGINL TDFAPPVEEM TTAPAELIAV SSH
//
