(data stored in ACNUC7421 zone)

HOGENOM: SHEDO_1_PE101

ID   SHEDO_1_PE101                        STANDARD;      PRT;   337 AA.
AC   SHEDO_1_PE101; Q12T28;
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;
DE   (SHEDO_1.PE101).
GN   Name=moaA; OrderedLocusNames=Sden_0101;
OS   SHEWANELLA DENITRIFICANS OS217.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SHEDO_1.PE101.
CC       Shewanella denitrificans OS217, complete genome.
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:MOAA_SHEDO
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: HOG000228682 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q12T28; -.
DR   EMBL; CP000302; ABE53398.1; -; Genomic_DNA.
DR   RefSeq; YP_561121.1; NC_007954.1.
DR   ProteinModelPortal; Q12T28; -.
DR   STRING; Q12T28; -.
DR   GeneID; 4017165; -.
DR   GenomeReviews; CP000302_GR; Sden_0101.
DR   KEGG; sdn:Sden_0101; -.
DR   NMPDR; fig|318161.14.peg.94; -.
DR   eggNOG; COG2896; -.
DR   OMA; LMKQYTA; -.
DR   PhylomeDB; Q12T28; -.
DR   ProtClustDB; PRK00164; -.
DR   BioCyc; SDEN318161:SDEN_0101-MON; -.
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; 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; FALSE_NEG.
DR   HOGENOMDNA; SHEDO_1.PE101; -.
KW   molybdenum cofactor biosynthesis protein A;
KW   4Fe-4S; Complete proteome; GTP-binding; Iron; Iron-sulfur;
KW   Metal-binding; Molybdenum cofactor biosynthesis; Nucleotide-binding;
KW   S-adenosyl-L-methionine.
SQ   SEQUENCE   337 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MHSPPALGKV NMSQLQDNFG RRFHYLRLSI TDACNFKCTY CLPDGYQSQG NSPFLSLSEI
     ELLLGAFSQM GTQKVRITGG EPSLRKDFID IIGLAANTPN IKTVATTTNG YRLAKNAQAW
     YDAGLRRINV SIDSLDPKMF YQITGENRFD QVMRGVDAAL ESGFERVKIN AVLLKGLNSQ
     DLPRFLHWIK HMPVDLRFIE LMETGLGREY FKAHHLAGTQ VKQQLIRDGW QLDKADILDG
     PAQNFSHSDY QGRIGLIMPY EKNFCVSCNR LRVSAKGQLH LCLFTENGVN LKDLLQDKSQ
     TPELMARLQQ QLGFKTAAHS LHQGITGVTT HLASIGG
//

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