ID Q0SHH6_RHOJR Unreviewed; 379 AA.
AC Q0SHH6;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=GTP cyclohydrolase 1 type 2 homolog {ECO:0000256|ARBA:ARBA00022112, ECO:0000256|PIRNR:PIRNR037489};
GN OrderedLocusNames=RHA1_ro01183 {ECO:0000313|EMBL:ABG93010.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG93010.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
CC {ECO:0000256|ARBA:ARBA00006964, ECO:0000256|PIRNR:PIRNR037489}.
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DR EMBL; CP000431; ABG93010.1; -; Genomic_DNA.
DR RefSeq; WP_011594287.1; NC_008268.1.
DR AlphaFoldDB; Q0SHH6; -.
DR KEGG; rha:RHA1_ro01183; -.
DR PATRIC; fig|101510.16.peg.1210; -.
DR eggNOG; COG0327; Bacteria.
DR eggNOG; COG3323; Bacteria.
DR HOGENOM; CLU_037423_1_1_11; -.
DR OrthoDB; 9795763at2; -.
DR Proteomes; UP000008710; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.120; -; 1.
DR Gene3D; 3.40.1390.30; NIF3 (NGG1p interacting factor 3)-like; 1.
DR InterPro; IPR002678; DUF34/NIF3.
DR InterPro; IPR017221; DUF34/NIF3_bac.
DR InterPro; IPR036069; DUF34/NIF3_sf.
DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR NCBIfam; TIGR00486; YbgI_SA1388; 1.
DR PANTHER; PTHR13799; NGG1 INTERACTING FACTOR 3; 1.
DR PANTHER; PTHR13799:SF13; NIF3-LIKE PROTEIN 1; 1.
DR Pfam; PF01784; DUF34_NIF3; 1.
DR PIRSF; PIRSF037489; UCP037489_NIF3_YqfO; 1.
DR SUPFAM; SSF102705; NIF3 (NGG1p interacting factor 3)-like; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRNR:PIRNR037489};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710}.
SQ SEQUENCE 379 AA; 39705 MW; 29297F1F466A7BD3 CRC64;
MNPVRLADVI AALDAAYPPA LAESWDSVGL VCGDPDDTVT TVTIAVDPTA EVVDEAIDAG
ADLLLVHHPL LLRGVDTVGA HTPKGALVHK LIKAGCALFT AHTNADSADP GVSDALAAAL
GLTVTGPIDP HPTEDLDKWV VLVPAGDADT VRRALFDAGA GHIGNYRNCS WSVTGQGQFL
PTDGANPTLG AVGALERVEE SRVEVIAPRG IRQKVLAAMR AAHPYEEVAF DVFEMATFPG
PRGLGRFGEL PEPLSLRDFT DRVADALPAT TWGVRAAGDP EATIRTVAVC GGSGDSYLDA
VSRLGVDAYV TADLRHHPAD EHLRAGGPAL IDVAHWASEQ PWCDQAKGVL DAAFGRTPEW
QVRVSAVRTD PWSVSASPS
//
