ID A0A495E6M7_9FLAO Unreviewed; 926 AA.
AC A0A495E6M7;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Aconitase {ECO:0000313|EMBL:RKR12219.1};
GN ORFNames=CLV91_2345 {ECO:0000313|EMBL:RKR12219.1};
OS Maribacter vaceletii.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Maribacter.
OX NCBI_TaxID=1206816 {ECO:0000313|EMBL:RKR12219.1, ECO:0000313|Proteomes:UP000269412};
RN [1] {ECO:0000313|EMBL:RKR12219.1, ECO:0000313|Proteomes:UP000269412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25230 {ECO:0000313|EMBL:RKR12219.1,
RC ECO:0000313|Proteomes:UP000269412};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (OCT-2018) 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 -!- 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:RKR12219.1}.
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DR EMBL; RBIQ01000009; RKR12219.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495E6M7; -.
DR OrthoDB; 9758061at2; -.
DR Proteomes; UP000269412; Unassembled WGS sequence.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000269412};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 6..163
FT /note="Aconitase B HEAT-like"
FT /evidence="ECO:0000259|Pfam:PF11791"
FT DOMAIN 182..408
FT /note="Aconitase B swivel"
FT /evidence="ECO:0000259|Pfam:PF06434"
FT DOMAIN 412..897
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
SQ SEQUENCE 926 AA; 101043 MW; 0B5CA46F3C482408 CRC64;
MTIYKDYIAE IEERKGQGLH PKPIDGADLL SAIIEQIKDV DNANREDSLN FFIYNVLPGT
TSAAGVKATF LKEIILGEEV VKEITPDFAL EQLSHMKGGP SVKVLLDLVL DQKDIDIAKK
SAEVLKTQVF LYEADTERLA DAMKKGCPIS KDIIESYAQA EFFTKLPDVD EEIEIVTYVA
GVGDISTDLL SPGADAHSRS DRELHGQCMF EHNKEMQNEV LALKEQHPDK RVMLIAEKGT
MGVGSSRMSG VNNVALWTGV PFSKYVPFIN YAPVIAGTNG IAPIFLTTVG VTGGIGIDLK
NWVTKKNADG NTVYVADGEP VLEQTYSVDT GTVLTINTKE KKLYKNGEAV KDISTALTPP
KMEFIKAGGS YAVVFGKKLQ TFACKVLGID VPQVYAAAKE VSVEGQGLTA VEKIFNKNAV
GTTPGKTLHA GSNVRVEVNI VGSQDTTGLM TSQELEMMAA TVISPIVDAG YQSGCHTASV
WDDKSKANIP RLMSFMNDFG LITGRDPKGK YFPMTDVIHK VLNDIAVDDW DVIIGGDSHT
RMAKGVAFGA DSGTVALALA TGEATMPIPQ SVKVTFKGNM KSYMDFRDVV HATQEQMLNQ
FGGENVFQGR IIEVHIGTLT SDEAFTFTDW TAEMKAKASI CISEDDTLAE SLAISRDRIQ
IMLDKGMDND KKVLQGLVDK ANKRIAELKS GERPALKPDA DAEYHAEVVI DLDKIVEPMI
ADPDVNNEDV SKRYTHDNIQ PLSFYGGTKK VDLGFVGSCM IHKGDMKILA QMLKNVEAQQ
GKVEFKAPLV VAPPTYNIVD ELKEEGDWEI LEKYSGFVFD DSAPKGLART KYENLLYLER
PGCNLCMGNQ EKAEPGDTVM ATSTRLFQGR VVRDTDGKKG ESLLSSTPVV VLSTILGRTP
TMEEYEAAVE GIVLTKFKPS QKQLVS
//
