(data stored in SCRATCH zone)

HOGENOM: GEKAU1_1_PE14

ID   GEKAU1_1_PE14                        STANDARD;      PRT;   341 AA.
AC   GEKAU1_1_PE14; Q5QL53;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Molybdenum cofactor biosynthesis protein A 2;
DE   (GEKAU1_1.PE14).
GN   Name=moaA2; OrderedLocusNames=GKP14;
OS   GEOBACILLUS KAUSTOPHILUS HTA426.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=235909;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS GEKAU1_1.PE14.
CC       Geobacillus kaustophilus HTA426 plasmid pHTA426, complete sequence.
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:Q5QL53_GEOKA
CC   -!- FUNCTION: Together with moaC, is involved in the conversion of a
CC       guanosine derivative (5'-GTP) into molybdopterin precursor Z (By
CC       similarity).
CC   -!- COFACTOR: Binds 2 4Fe-4S clusters. Binds 1 4Fe-4S cluster
CC       coordinated with 3 cysteines and an exchangeable S-adenosyl-L-
CC       methionine and 1 4Fe-4S cluster coordinated with 3 cysteines and
CC       the GTP-derived substrate (By similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC   -!- SUBUNIT: Monomer and homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. MoaA family.
CC   -!- GENE_FAMILY: HOG000228681 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q5QL53; -.
DR   EMBL; AP006520; BAD74257.1; -; Genomic_DNA.
DR   RefSeq; YP_145825.1; NC_006509.1.
DR   ProteinModelPortal; Q5QL53; -.
DR   SMR; Q5QL53; 8-331.
DR   GeneID; 3170873; -.
DR   GenomeReviews; AP006520_GR; GKP14.
DR   KEGG; gka:GKP14; -.
DR   NMPDR; fig|235909.3.peg.42; -.
DR   OMA; MENERAY; -.
DR   ProtClustDB; CLSK2395610; -.
DR   GO; GO:0019008; C:molybdopterin synthase complex; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_01225_B; MoaA_B; 1; -.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR013483; MoaA.
DR   InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
DR   InterPro; IPR010505; Mob_synth_C.
DR   InterPro; IPR007197; rSAM.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   Pfam; PF06463; Mob_synth_C; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR02666; MoaA; 1.
DR   PROSITE; PS01305; MOAA_NIFB_PQQE; 1.
DR   HOGENOMDNA; GEKAU1_1.PE14; -.
KW   molybdopterin cofactor biosynthesis protein;
KW   4Fe-4S; Complete proteome; GTP-binding; Iron; Iron-sulfur;
KW   Metal-binding; Molybdenum cofactor biosynthesis; Nucleotide-binding;
KW   Plasmid; S-adenosyl-L-methionine.
SQ   SEQUENCE   341 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MEERDRVKIT DRLARPLRDL RLSVTDQCNF RCVYCMPAEV FGPNFRFLDE GQLLTVEEMA
     LLAECFVELG VEKIRLTGGE PLLRRDLDAL IERLSAIPGL RDIGLTTNGV HLVKWSKRLK
     AAGLKRVNVS LDALDDDIFR KMNGIGVGAA PVLKGIEAAL AAGLGVKVNM VVKKGWNDSQ
     IVPMAAYFKD LGIPLRFIEF MDVGTTNGWD YSHVVTKKEI YEQINAMHPL EPVEKEYFGE
     VANRYRYAGT NVEVGFIASV TETFCRSCTR ARISADGKLY TCLFAADGVS LKDKLRAGAE
     KEELKALIAA VWSKRADRYS EERTAETAKQ RPKIEMSYIG G
//

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