ID K1M962_9FLAO Unreviewed; 921 AA.
AC K1M962;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Aconitate hydratase 2 {ECO:0000313|EMBL:EKB58913.1};
GN ORFNames=HMPREF9699_00458 {ECO:0000313|EMBL:EKB58913.1};
OS Bergeyella zoohelcum ATCC 43767.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Bergeyella.
OX NCBI_TaxID=883096 {ECO:0000313|EMBL:EKB58913.1, ECO:0000313|Proteomes:UP000006085};
RN [1] {ECO:0000313|EMBL:EKB58913.1, ECO:0000313|Proteomes:UP000006085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43767 {ECO:0000313|EMBL:EKB58913.1,
RC ECO:0000313|Proteomes:UP000006085};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bergeyella zoohelcum ATCC 43767.";
RL Submitted (JUL-2012) 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:EKB58913.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGYA01000008; EKB58913.1; -; Genomic_DNA.
DR RefSeq; WP_002662081.1; NZ_JH932293.1.
DR AlphaFoldDB; K1M962; -.
DR STRING; 883096.HMPREF9699_00458; -.
DR PATRIC; fig|883096.3.peg.466; -.
DR eggNOG; COG1049; Bacteria.
DR HOGENOM; CLU_314657_0_0_10; -.
DR OrthoDB; 9758061at2; -.
DR Proteomes; UP000006085; 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:UP000006085};
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 176..404
FT /note="Aconitase B swivel"
FT /evidence="ECO:0000259|Pfam:PF06434"
FT DOMAIN 410..894
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
SQ SEQUENCE 921 AA; 100694 MW; 8F328C06DD0D8F8A CRC64;
MNLYNDYIQE IEERKQQGLH PKPIDGAELL SEIIEQIKDE NSSHRADAIH HFIYNTLPGT
TSAAGVKAQF LKDIVLGKEN IAEISTDFAF ELLSHMKGGP SIKVLLDLAL GNDEAIAQKA
AEVLKTQVFL YDADTARLAE AYKAGNAIAK DILKSYAKAE FFTQLPEVPE EIKVVTYIAA
EGDISTDLLS PGNQAHSRSD RELHGKSMIS PEAQAEIVAM KAAHPDKQVM LIAEKGTMGV
GSSRMSGVNN VALWTGKQAS PYVPFVNIAP IVAGTNGISP IFLTTVDVTG GIGIDLQNWV
KKTDADGNVV RDEKGDIILE QVYSVETGTV LTINTKTKKL YNGDQELKDI SKSFTPQKLE
FIRAGGSYAI VFGKKIQTFA AQTLGIQAPQ VFAPAKEVVK EGVGLTAVEK IFNKNAVGVA
PGKTLYAGSD VRVKVNIVGS QDTTGLMTAQ ELEAMAATVI SPIVDGAYQS GCHTASVWDK
KAQANIPKLM KFMNDFGVIT ARDPKGEYHA MTDVIHKVLN DITVDEWAII IGGDSHTRMS
KGVAFGADSG TVALALATGE ASMPIPESVK VTFKGSMKEH MDFRDVVHAT QLQMLQQFDG
ENVFQGRIIE VHIGTLLADQ AFTFTDWTAE MKAKASICIS QDDTLIESLE IAKSRIQIMI
EKGMDNENQV LKGLIAKADK RIAEIRSGEK PALQPDADAK YYAEVVIDLD LIDEPMIADP
DVNNEDISKR YTHDTIRPLS FYGDNKKVDL GFVGSCMVHK DDLKIVSQML KNLEKQYGEV
KFNAPLVVAA PTYNIIDELK AEGDWEYLQK YSGFEFSDAL PKQTARTEYE NIMYLERPGC
NLCMGNQEKA EKGDTVMSTS TRLFQGRVVE DRADKKGESL LASTPVVVLS AILGRIPTME
EYKVAVEGIN LTKFQPISTK I
//
