ID A0A1V3LD29_9PAST Unreviewed; 867 AA.
AC A0A1V3LD29;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=BKG88_00435 {ECO:0000313|EMBL:OOF88148.1};
OS Rodentibacter ratti.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Rodentibacter.
OX NCBI_TaxID=1906745 {ECO:0000313|EMBL:OOF88148.1, ECO:0000313|Proteomes:UP000189353};
RN [1] {ECO:0000313|EMBL:OOF88148.1, ECO:0000313|Proteomes:UP000189353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ppn158 {ECO:0000313|EMBL:OOF88148.1,
RC ECO:0000313|Proteomes:UP000189353};
RA Christensen H.;
RT "Rodentibacter gen. nov. and new species.";
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}.
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:OOF88148.1}.
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DR EMBL; MLAI01000002; OOF88148.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3LD29; -.
DR OrthoDB; 9758061at2; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000189353; 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: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.
DR PROSITE; PS01244; ACONITASE_2; 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|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR036687};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036687-1};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|PIRNR:PIRNR036687}.
FT DOMAIN 6..158
FT /note="Aconitase B HEAT-like"
FT /evidence="ECO:0000259|Pfam:PF11791"
FT DOMAIN 171..384
FT /note="Aconitase B swivel"
FT /evidence="ECO:0000259|Pfam:PF06434"
FT DOMAIN 474..820
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT BINDING 246..248
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT BINDING 416..418
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT BINDING 500
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT BINDING 712
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-1"
FT BINDING 771
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-1"
FT BINDING 774
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-1"
FT BINDING 793
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT BINDING 798
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
SQ SEQUENCE 867 AA; 94752 MW; E0EBA7F828DC8A77 CRC64;
MSFLTEYQTH VNQRAAQGVV PLPLNAQQTA ELVELLKNPP PENQNLLVEL FESRIPTGVD
EAAYVKAAFL ADLIKGNTQS PLISPQKAVQ LLGTMQGGYN IEPLIDTLEI DELAPLAVKA
LSHTLLMFDN FYDVAQKAKQ GNTYALQILQ SWADAKWFLS RPQLAEKLTY TVFKVSGETN
TDDLSPAQDA WSRPDIPLHA LAMLKNPREG IEPDEVGVIG PMKQIESLKQ KGFPLVYVGD
VVGTGSSRKS ATNSVLWLMG EDMPYIPNKR TGGIVLGGKI APIFFNTMED AGALPIELDV
SRLNMGDVID IYPYAGKVCK HNTDEVLSTF KLKTDVLLDE VRAGGRIPLI IGRGLTHKAR
VELGLSESDV FAKPQVSNEN NKGFTLAQKI VGRACGVTGI RAGQYCEPRM TSVGSQDTTG
PMTRDELKDL ACLGFSADLV MQSFCHTAAY PKPVDVVTHH SLPDFIMNRG GVSLRPGDGV
IHSWLNRMLL PDTVGTGGDS HTRFPIGISF PAGSGLVAFA AATGVMPLDM PESVLIRFSG
EMQAGITLRD LVHAIPYYAI QQGLLTVEKA GKKNIFSGKI LEIEGLEHLK VEQAFEISDA
SAERSAAACS IKLNKEPIIE YLNSNIVLLK WMIAEGYGDK TTLERRIKAM QDWLANPQLL
EADKDAEYAA VIEINLNDIK EPIVCAPNDP DDARLLSEVQ DDKVDEVFIG SCMTNIGHFR
AAGKLLNQHQ GMIPTRLWIV PPTKMDAHLL SDEGYYSIYG KSGARIEVPG CSLCMGNQAR
VADGATVVST STRNFPNRMG KGAFVYLASA ELSAVCALLG RIPTAEEYLQ YVQSLEADKD
DTYRYMNFDQ IDHYSNKVNG LIFQTAV
//
