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Database: UniProt
Entry: A0A1G8LPV9_9RHOO
LinkDB: A0A1G8LPV9_9RHOO
Original site: A0A1G8LPV9_9RHOO 
ID   A0A1G8LPV9_9RHOO        Unreviewed;       910 AA.
AC   A0A1G8LPV9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Aconitate hydratase B {ECO:0000256|ARBA:ARBA00019379, ECO:0000256|PIRNR:PIRNR036687};
DE            EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926, ECO:0000256|PIRNR:PIRNR036687};
DE            EC=4.2.1.99 {ECO:0000256|ARBA:ARBA00013250, ECO:0000256|PIRNR:PIRNR036687};
DE   AltName: Full=2-methylisocitrate dehydratase {ECO:0000256|PIRNR:PIRNR036687};
GN   ORFNames=SAMN05660652_03673 {ECO:0000313|EMBL:SDI57665.1};
OS   Propionivibrio dicarboxylicus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Propionivibrio.
OX   NCBI_TaxID=83767 {ECO:0000313|EMBL:SDI57665.1, ECO:0000313|Proteomes:UP000198607};
RN   [1] {ECO:0000313|EMBL:SDI57665.1, ECO:0000313|Proteomes:UP000198607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5885 {ECO:0000313|EMBL:SDI57665.1,
RC   ECO:0000313|Proteomes:UP000198607};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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         ECO:0000256|PIRNR:PIRNR036687};
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         ECO:0000256|PIRNR:PIRNR036687};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|PIRSR:PIRSR036687-1};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000256|PIRSR:PIRSR036687-1};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC       from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717,
CC       ECO:0000256|PIRNR:PIRNR036687}.
CC   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC       {ECO:0000256|ARBA:ARBA00005026}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|PIRNR:PIRNR036687}.
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DR   EMBL; FNCY01000022; SDI57665.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8LPV9; -.
DR   STRING; 83767.SAMN05660652_03673; -.
DR   UniPathway; UPA00223; UER00718.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000198607; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd01581; AcnB; 1.
DR   CDD; cd01576; AcnB_Swivel; 1.
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; IPR018136; Aconitase_4Fe-4S_BS.
DR   InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR   InterPro; IPR004406; Aconitase_B.
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   NCBIfam; TIGR00117; acnB; 1.
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   PIRSF; PIRSF036687; AcnB; 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.
DR   PROSITE; PS00450; ACONITASE_1; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRSR:PIRSR036687-1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR036687-1};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR036687-
KW   1}; Lyase {ECO:0000256|PIRNR:PIRNR036687};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR036687-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198607};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|PIRNR:PIRNR036687}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..910
FT                   /note="Aconitate hydratase B"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011764343"
FT   DOMAIN          61..213
FT                   /note="Aconitase B HEAT-like"
FT                   /evidence="ECO:0000259|Pfam:PF11791"
FT   DOMAIN          225..437
FT                   /note="Aconitase B swivel"
FT                   /evidence="ECO:0000259|Pfam:PF06434"
FT   DOMAIN          511..874
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   BINDING         248
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT   BINDING         301..303
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT   BINDING         472..474
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT   BINDING         556
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT   BINDING         768
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036687-1"
FT   BINDING         825
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036687-1"
FT   BINDING         828
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036687-1"
FT   BINDING         847
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT   BINDING         852
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
SQ   SEQUENCE   910 AA;  97141 MW;  46DEEDBBF398304E CRC64;
     MLNRRSFCIR SAATVAAAVS INGVAEAAPG ATQRNAAAGG SAASPGLVID EATARSTILD
     AYRKHVAERA AQGLPPLSLN PVQTAAVAVL LKNPPKGEEA FLLDLLSTRV PPGVDAAAKV
     KADFLATIAT GKDKSPVITR QKAVELLGTM QGGYNVKTLI ALLGDPTLGT AAADCLKKTL
     LIFGAIKDVK ALADKGNANA KGVLKSWAEG EWFSARADVP KSIKLTVFKV GGETNTGDLS
     PDPDANTRTD IPLHAQAILK FPRAGLTPDE PGKRGPLKQF EAMKAKGNPL VYVGDVVGPG
     SSRKSATNSL LWMTGQDIPF VPNKRFGGFV FAGKIAPIFY NTMQDSGALP IEMDVSKLEM
     GDVIELLPFD GKVLKNGEVV ASFKLKTDVL LDSVRAGGRI PLIIGRNLTA EARKMLGMSA
     TAMFRAPKQP ADTGKGYTLA QKIVGRACGL PAGKGVRPGT YCEPVMDTIG SQDTIGPMTR
     DEQNDLACLS FSADLVLQTF CHTAAYPKPE DVKMYAELPQ YIYSRGGVAV RPGDGVLHSW
     LNRMAMPDSV GTGGDSHTRF PIGVYFPAGS GLCALASATG VMPLDMPESV LVRFKGEMQA
     GVTLRDLVNA IPYYAFRQGL LTVDKKGKKN IFSGRILEIE GLPNLTVEQA FEISDASAER
     SAEACTVRLG KEPIVEYMQS NVALLKWMVA NGYQDRNALL RRIAKMEAWL KNPQIQEPDA
     NAEYAAVIEI NLAEVTEPLL ACPNDPDDIK PLSAVAGAKV DEGFIGSCQT NIGHFRAAAH
     ILKGKELPTR LWVVPPTKMD ADTLNREGYY ATLGEAGARM EVPGCSLCFG NQARARKGAT
     VVSTSTRNFP NRMGTGTNVY LASAEVTAVA SLLGKIPTKA EYLEHMKVVQ QKAADIYRYM
     NFHQMAEFKA
//
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