ID A0A1H6Z0P2_9PSED Unreviewed; 866 AA.
AC A0A1H6Z0P2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=SAMN03159495_3320 {ECO:0000313|EMBL:SEJ43100.1};
OS Pseudomonas sp. NFR16.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1566248 {ECO:0000313|EMBL:SEJ43100.1, ECO:0000313|Proteomes:UP000199219};
RN [1] {ECO:0000313|EMBL:SEJ43100.1, ECO:0000313|Proteomes:UP000199219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NFR16 {ECO:0000313|EMBL:SEJ43100.1,
RC ECO:0000313|Proteomes:UP000199219};
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; FNYJ01000003; SEJ43100.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6Z0P2; -.
DR STRING; 1566248.SAMN03159495_3320; -.
DR OrthoDB; 9758061at2; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000199219; 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.
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 4..156
FT /note="Aconitase B HEAT-like"
FT /evidence="ECO:0000259|Pfam:PF11791"
FT DOMAIN 169..382
FT /note="Aconitase B swivel"
FT /evidence="ECO:0000259|Pfam:PF06434"
FT DOMAIN 471..818
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT BINDING 244..246
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT BINDING 414..416
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT BINDING 498
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT BINDING 710
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-1"
FT BINDING 769
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-1"
FT BINDING 772
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-1"
FT BINDING 791
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT BINDING 796
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
SQ SEQUENCE 866 AA; 93534 MW; DDFE6A86BF10F9D2 CRC64;
MLEAYRKHIE ERAAQGIVPQ PLNAEQTAGL VELLKNPPAG EEAVLLDLIT NRVPPGVDEA
AYVKAGFLSA LAKGEVTSPL LDKKRAVELL GTMQGGYNIV TMVDLLDHAE LAPVAAEQLK
HTLLMFDAFH DVAEKAKNGN AHAQAVLQSW ADGEWFQKRP TLAEKISLRV FKVTGETNTD
DLSPAPDAWS RPDIPLHALA MLKMARDGIV PDVQGSIGPM KQIEEMRGQG FPIAYVGDVV
GTGSSRKSAT NSVLWFFGDD VPYVPNKRAG GFCFGSKIAP IFYNTMEDAG ALPIEFDVSS
INMGDVIDVY PYAGKVCKHD SDEVITTFEL KTPVLLDEVR AGGRIPLIIG RGLTGKARAE
LGLPPSTLFK LPEVPAASTK GFTLAQKMVG KACGTDGIRP GTYCEPKMTT VGSQDTTGPM
TRDELKDLAC LGFSTDLVMQ SFCHTAAYPK PIDVKTHHTL PDFIMTRGGV SLRPGDGIIH
SWLNRMLLPD TVGTGGDSHT RFPIGISFPA GSGLVAFAAA TGVMPLDMPE SILVRFKGKL
QPGVTLRDLV HAIPYYAIQK GLLTVEKKGK KNAFSGRILE IEGLETLTVE QAFELSDASA
ERSAAGCTIK LSKESIAEYL KSNITLLRWM IGEGYGDPRT LERRAQAMEA WVANPELLEA
DADAEYAEVI EIDLADVKEP VLCAPNDPDD ARLLSSVAGE KIDEVFIGSC MTNIGHFRAA
GKLLDQVKGQ LPTRLWLSPP TKMDAHQLTE EGYYGIYGKA GARMEMPGCS LCMGNQARVE
PNSTVVSTST RNFPNRLGDG ANVYLASAEL ASVASILGRL PTVEEYMEYA GKIDSMAADV
YRYLSFDQIA EFREIAANAN IPVVQA
//
