ID A0ZF76_NODSP Unreviewed; 574 AA.
AC A0ZF76;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000313|EMBL:AHJ31223.1};
DE EC=4.2.1.33 {ECO:0000313|EMBL:AHJ31223.1};
GN ORFNames=NSP_49310 {ECO:0000313|EMBL:AHJ31223.1};
OS Nodularia spumigena CCY9414.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Nodularia.
OX NCBI_TaxID=313624 {ECO:0000313|EMBL:AHJ31223.1, ECO:0000313|Proteomes:UP000019325};
RN [1] {ECO:0000313|EMBL:AHJ31223.1, ECO:0000313|Proteomes:UP000019325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCY9414 {ECO:0000313|EMBL:AHJ31223.1};
RX PubMed=23555932;
RA Voss B., Bolhuis H., Fewer D.P., Kopf M., Moke F., Haas F., El-Shehawy R.,
RA Hayes P., Bergman B., Sivonen K., Dittmann E., Scanlan D.J., Hagemann M.,
RA Stal L.J., Hess W.R.;
RT "Insights into the physiology and ecology of the brackish-water-adapted
RT Cyanobacterium Nodularia spumigena CCY9414 based on a genome-transcriptome
RT analysis.";
RL PLoS ONE 8:E60224-E60224(2013).
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DR EMBL; CP007203; AHJ31223.1; -; Genomic_DNA.
DR RefSeq; WP_006196336.1; NZ_CP007203.1.
DR AlphaFoldDB; A0ZF76; -.
DR STRING; 313624.NSP_49310; -.
DR GeneID; 78016317; -.
DR PATRIC; fig|313624.11.peg.4939; -.
DR eggNOG; COG0065; Bacteria.
DR eggNOG; COG0066; Bacteria.
DR HOGENOM; CLU_006714_3_4_3; -.
DR Proteomes; UP000019325; Chromosome.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:InterPro.
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:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR CDD; cd01583; IPMI; 1.
DR CDD; cd01577; IPMI_Swivel; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 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; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR InterPro; IPR011826; HAcnase/IPMdehydase_lsu_prok.
DR InterPro; IPR006251; Homoacnase/IPMdehydase_lsu.
DR InterPro; IPR033941; IPMI_cat.
DR InterPro; IPR033940; IPMI_Swivel.
DR NCBIfam; TIGR01343; hacA_fam; 1.
DR NCBIfam; TIGR02086; IPMI_arch; 1.
DR PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AHJ31223.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 57..103
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT DOMAIN 171..567
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
SQ SEQUENCE 574 AA; 62338 MW; AE457F7F41D2D023 CRC64;
MSSINKEVTK KVLYLGDDIN TDDIIPANRA TTYDPDILKQ YALEHLIGVG ELLKYNVIVA
GENFGCGSSR EIAPVALKAA GIEKIQARSF AEIFYRNSIN IGLNLEILEE KQENPVVEAI
AQAGGLIPFN QMRRQGKITT PKSVTPQRPM TLVEKLIAKA SGNTYVRPGE VVFAQVDLAL
SHDAVAGPVA TTFYKHYGKE AKLWDAQRVV LVADHFIQVN DIRNDQKANV MYQEMIDFAK
KQGCHLFDIV SPGEAAGICH VLLPEKGFVR PGMIIAGTDS HTCTYGALGA FSAGVGTTDM
ANIYAMGDMW IRVPSTLVFE LSGTLPPHIS AKDIILFILG QIGCAGATSK VMEFRGSILE
QMPFDERLTL ANMAIECGAI CGLIVPDETT RNYVRSRSDQ EFEELIADPD AEYEKVYKFD
ISNLEPQIAR PPKPDQVVPI SQIEETPITK AFIGSCTGGK LYDLAQAAEV LQDRQVADGV
NLFIVPASVE IREKAEALGY MDIFAQAGAK ILKSGCGACI NSGIGVLNKE ETGVYATNRN
FKGRSGDPTG KNYLASPRTV AISAVKGKIS HILD
//
