GCHK_ANADF
ID GCHK_ANADF Reviewed; 382 AA.
AC A7HD43;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Globin-coupled histidine kinase {ECO:0000303|PubMed:21852234};
DE EC=2.7.13.3 {ECO:0000269|PubMed:21852234, ECO:0000269|PubMed:26212354};
DE AltName: Full=AfGcHK {ECO:0000303|PubMed:21852234, ECO:0000303|PubMed:26212354};
DE AltName: Full=Heme-based oxygen-sensor histidine kinase {ECO:0000303|PubMed:21852234};
GN Name=gchK {ECO:0000303|PubMed:21852234}; OrderedLocusNames=Anae109_2438;
OS Anaeromyxobacter sp. (strain Fw109-5).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC unclassified Anaeromyxobacter.
OX NCBI_TaxID=404589;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fw109-5;
RX PubMed=25614562; DOI=10.1128/genomea.01449-14;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA Loeffler F.E., Fields M.W.;
RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT metal-reducing bacterium isolated from a contaminated subsurface
RT environment.";
RL Genome Announc. 3:0-0(2015).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, HEME-BINDING,
RP OXYGEN-BINDING, RESONANCE RAMAN SPECTROSCOPY, PTM, PHOSPHORYLATION AT
RP HIS-183, SUBUNIT, GENE NAME, MUTAGENESIS OF TYR-45; HIS-99 AND HIS-183, AND
RP DOMAIN.
RC STRAIN=Fw109-5;
RX PubMed=21852234; DOI=10.1074/jbc.m111.274811;
RA Kitanishi K., Kobayashi K., Uchida T., Ishimori K., Igarashi J.,
RA Shimizu T.;
RT "Identification and functional and spectral characterization of a globin-
RT coupled histidine kinase from Anaeromyxobacter sp. Fw109-5.";
RL J. Biol. Chem. 286:35522-35534(2011).
RN [3]
RP AUTOPHOSPHORYLATION ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, MUTAGENESIS OF HIS-99, AND DOMAIN.
RC STRAIN=Fw109-5;
RX PubMed=26212354; DOI=10.1021/acs.biochem.5b00517;
RA Fojtikova V., Stranava M., Vos M.H., Liebl U., Hranicek J., Kitanishi K.,
RA Shimizu T., Martinkova M.;
RT "Kinetic analysis of a globin-coupled histidine kinase, AfGcHK: Effects of
RT the heme iron complex, response regulator, and metal cations on
RT autophosphorylation activity.";
RL Biochemistry 54:5017-5029(2015).
CC -!- FUNCTION: Member of the two-component regulatory system
CC GcHK/Anae109_2439. Autophosphorylates in response to oxygen
CC availability, and then transfers the phosphate group to a conserved Asp
CC residue in the receiver domains of the cognate response regulator
CC Anae109_2439, resulting in its activation.
CC {ECO:0000269|PubMed:21852234}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:21852234,
CC ECO:0000269|PubMed:26212354};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:21852234};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000269|PubMed:21852234};
CC -!- ACTIVITY REGULATION: Gas or ligand binding and heme iron redox state
CC regulate the histidine kinase activity: heme-free AfGcHK and the heme
CC Fe(II) complex are less active forms, whereas the heme Fe(III)-OH(-),
CC Fe(III)-CN(-), Fe(III)-imidazole, Fe(II)-CO, and Fe(II)-O(2) complexes
CC are active forms. The activation of the functional domain seems to be
CC dependent on the formation of a six-coordinate low-spin heme iron
CC complex. Mg(2+) ions, and to a lesser extent, Mn(2+) ions, enhance the
CC autophosphorylation reaction, although the presence of a divalent metal
CC ion does not appear to be essential for the reaction. Co(2+), Ni(2+),
CC Zn(2+), and Cd(2+) totally inhibit autophosphorylation activity.
CC {ECO:0000269|PubMed:21852234, ECO:0000269|PubMed:26212354}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18.9 uM for ATP (with the Fe(III)-OH(-) bound form of the enzyme)
CC {ECO:0000269|PubMed:26212354};
CC KM=35.4 uM for ATP (with the Fe(III)-CN(-) bound form of the enzyme)
CC {ECO:0000269|PubMed:26212354};
CC KM=23.8 uM for ATP (with the Fe(III)-imidazole bound form of the
CC enzyme) {ECO:0000269|PubMed:26212354};
CC KM=23.0 uM for ATP (with the Fe(II)-O(2) bound form of the enzyme)
CC {ECO:0000269|PubMed:26212354};
CC KM=357.0 uM for ATP (with the Fe(II)-CO bound form of the enzyme)
CC {ECO:0000269|PubMed:26212354};
CC KM=78 uM for ATP (with the Fe(II) bound form of the enzyme)
CC {ECO:0000269|PubMed:26212354};
CC KM=33.6 uM for ATP (with the heme-free form of the enzyme)
CC {ECO:0000269|PubMed:26212354};
CC Note=kcat is 1.1 min(-1) for the autophosphorylation reaction with
CC the Fe(III)-OH(-) bound form of the enzyme. kcat is 1.2 min(-1) with
CC the Fe(III)-CN(-) bound form of the enzyme. kcat is 1.1 min(-1) with
CC the Fe(III)-imidazole bound form of the enzyme. kcat is 1.0 min(-1)
CC with the Fe(II)-O(2) bound form of the enzyme. kcat is 1.0 min(-1)
CC with the Fe(II)-CO bound form of the enzyme. kcat is 0.4 min(-1) with
CC the Fe(II) bound form of the enzyme. kcat is 0.3 min(-1) with the
CC heme-free form of the enzyme. The presence of the cognate response
CC regulator (RR) protein significantly reduces the enzyme affinity for
CC ATP. {ECO:0000269|PubMed:26212354};
CC pH dependence:
CC Optimum pH is around 11.0 for the autophosphorylation reaction with
CC the Fe(III)-OH(-) bound form of the enzyme. At pH 8.0, displays 75%
CC of the optimal rate. Is inactive below pH 5.5 and above pH 12.7.
CC {ECO:0000269|PubMed:26212354};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21852234}.
CC -!- DOMAIN: Consists of two domains: an N-terminal heme-based oxygen-sensor
CC domain, and a C-terminal catalytic domain that exhibits histidine
CC kinase activity (PubMed:21852234). The coordination and oxidation state
CC of the sensor domain heme iron profoundly affect the enzyme's catalytic
CC activity (PubMed:26212354). {ECO:0000269|PubMed:26212354,
CC ECO:0000305|PubMed:21852234}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:21852234,
CC ECO:0000269|PubMed:26212354}.
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DR EMBL; CP000769; ABS26639.1; -; Genomic_DNA.
DR PDB; 5OHE; X-ray; 1.85 A; A/B/C/D/E/F/G/H=2-161.
DR PDB; 5OHF; X-ray; 1.80 A; A/B/C/D/E/F/G/H=2-161.
DR PDB; 6OTD; X-ray; 1.80 A; A=2-161.
DR PDBsum; 5OHE; -.
DR PDBsum; 5OHF; -.
DR PDBsum; 6OTD; -.
DR AlphaFoldDB; A7HD43; -.
DR SMR; A7HD43; -.
DR STRING; 404589.Anae109_2438; -.
DR iPTMnet; A7HD43; -.
DR EnsemblBacteria; ABS26639; ABS26639; Anae109_2438.
DR KEGG; afw:Anae109_2438; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_722883_0_0_7; -.
DR OMA; HYMFGAM; -.
DR SABIO-RK; A7HD43; -.
DR Proteomes; UP000006382; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019825; F:oxygen binding; IDA:UniProtKB.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0018106; P:peptidyl-histidine phosphorylation; IDA:UniProtKB.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IDA:UniProtKB.
DR CDD; cd01068; globin_sensor; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.490.10; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR044398; Globin-sensor_dom.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR039379; Protoglobin_sensor_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF11563; Protoglobin; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Heme; Iron; Kinase; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..382
FT /note="Globin-coupled histidine kinase"
FT /id="PRO_5000267182"
FT DOMAIN 180..382
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107,
FT ECO:0000305|PubMed:21852234"
FT REGION 1..155
FT /note="Globin sensor"
FT /evidence="ECO:0000305|PubMed:21852234"
FT BINDING 45
FT /ligand="O2"
FT /ligand_id="ChEBI:CHEBI:15379"
FT /evidence="ECO:0000269|PubMed:21852234"
FT BINDING 99
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000269|PubMed:21852234"
FT MOD_RES 183
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107,
FT ECO:0000269|PubMed:21852234"
FT MUTAGEN 45
FT /note="Y->F: 3.5-fold increase in O(2) dissociation rate
FT constant. No effect on O(2) association rate constant."
FT /evidence="ECO:0000269|PubMed:21852234"
FT MUTAGEN 45
FT /note="Y->L: 80-fold increase in O(2) dissociation rate
FT constant. No effect on O(2) association rate constant."
FT /evidence="ECO:0000269|PubMed:21852234"
FT MUTAGEN 45
FT /note="Y->W: 34-fold increase in O(2) dissociation rate
FT constant. No effect on O(2) association rate constant."
FT /evidence="ECO:0000269|PubMed:21852234"
FT MUTAGEN 99
FT /note="H->A: Loss of heme-binding ability. 4-fold decrease
FT in autophosphorylation reaction rate and 2-fold decrease in
FT affinity for ATP."
FT /evidence="ECO:0000269|PubMed:21852234,
FT ECO:0000269|PubMed:26212354"
FT MUTAGEN 183
FT /note="H->A: Loss of autophosphorylation. Does not
FT significantly alter the O(2) and CO binding kinetic
FT values."
FT /evidence="ECO:0000269|PubMed:21852234"
FT HELIX 8..16
FT /evidence="ECO:0007829|PDB:5OHF"
FT HELIX 20..33
FT /evidence="ECO:0007829|PDB:5OHF"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:5OHF"
FT HELIX 37..49
FT /evidence="ECO:0007829|PDB:5OHF"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:5OHF"
FT HELIX 61..81
FT /evidence="ECO:0007829|PDB:5OHF"
FT HELIX 86..101
FT /evidence="ECO:0007829|PDB:5OHF"
FT HELIX 107..128
FT /evidence="ECO:0007829|PDB:5OHF"
FT HELIX 132..156
FT /evidence="ECO:0007829|PDB:5OHF"
SQ SEQUENCE 382 AA; 41941 MW; D007A082ABD1F8EA CRC64;
MTGVPETVFE ELKRYVGWGD GDERALRSLH GAAAPHFPRL AEEFYDRILG HEGARTALVG
GESQVGHLKV TMIAWLDELL GGPWDEAYWD RRYRIGRVHV RIGLPQHYMF GAMNVHRTGL
ARLAYERFHG DPPELERVRN ALGKVLDLEL AVMLHTYRED LLAQQARVER LSTFGQLVGS
IGHDLRNPLG VIETSLYILR TRTGEDERAR KHLDRIGEQL GVANGIITNL LDMIRDRPLA
REPVELAAVV GGAAESVRRP TGVSLALEGL DALPPVEGDP GQLRQVFVNL LENAVFAASP
EGVVAVRASR ADGLVALDVE DSGPGVDPAT RRRLFEPLIT TKDKGIGLGL ALVKRIAERH
GGTVEYSDRP GGGARFTVRL PA
